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Information on EC 2.4.1.25 - 4-alpha-glucanotransferase
for references in articles please use BRENDA:EC2.4.1.25
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EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.1 Hexosyltransferases
2.4.1.25 4-alpha-glucanotransferase
IUBMB Comments
This entry covers the former separate entry for EC 2.4.1.3 (amylomaltase). The plant enzyme has been termed D-enzyme. An enzymic activity of this nature forms part of the mammalian and yeast glycogen debranching system (see EC 3.2.1.33 amylo-α-1,6-glucosidase).
The enzyme appears in viruses and cellular organisms
- 2.4.1.25
- starch
- maltose
- maltodextrins
- amylose
-
transglycosylation
- glucans
- amylopectin
- cycloamylose
-
disproportionation
- malto-oligosaccharides
- maltotetraose
- maltohexaose
- alpha-glucans
- maltopentaose
- synthesis
- alpha-amylases
- amylo-1,6-glucosidase
-
maltogenic
-
malpq
-
large-ring
- alpha-1,4-glucans
- biotechnology
- nutrition
- medicine
- analysis
- food industry
showSynonyms
amylomaltase, d-enzyme, 4-alpha-glucanotransferase, disproportionating enzyme, amase, maltosyltransferase, alphagt, mq-01, alphagtase, alpha-1,4-glucanotransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-alpha-glucanotransferase
4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic
4-alpha-glucanotransferase DPE2
4-alpha-GTase
4alpha-GTase
4alphaGT
4alphaGTase
AMase
amylmaltase
amylomaltase
CgAM
Cqm1
the ordered domain (residues 23-560) of surface receptor protein Cqm1 has amylomaltase activity
D-enzyme
debranching enzyme
debranching enzyme maltodextrin glycosyltransferase
-
-
-
-
dextrin glycosyltransferase
-
-
-
-
dextrin glycosyltransferase,
-
-
-
-
dextrin transglycosylase
-
-
-
-
disproportionating enzyme
DPE1
DPE2
EC 2.4.1.3
-
-
formerly
-
exo-MGTase
GDE
GH77
GH77 amylomaltase
glycogen debranching enzyme
GTase
MalQ
maltodextrin glycosyltransferase
maltosyltransferase
MeDPE1
MgtA
MmtA
MTase
oligo-1,4-1,4-glucantransferase
Pcal_0768
prokaryotic 4-alpha-glucanotransferase
PyAMase
Sde_0986
TAalphaGT
TaAM
TLGT
TreX
additional information
4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic
-
amylomaltase
-
-
-
-
amylomaltase
-
D-enzyme
-
-
-
-
disproportionating enzyme
-
-
-
-
TreX
-
enzyme displays isoamylase and 4-alpha-glucanotransferase activity
additional information
the enzyme belongs to the glycoside hydrolase family 77, together with GH13 and GH70, it forms the clan GH-H, known as the alpha-amylase family
additional information
-
amylomaltase is a member of the 4-alpha-glucanotransferase family
additional information
amylomaltases are glycosyl hydrolases belonging to glycoside hydrolase family 77
additional information
the enzyme belongs to the glycoside hydrolase family 77, GH77, which belongs to the alpha-amylase superfamily, Clan H, together with GH13 and GH70
additional information
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
the enzyme belongs to the glycoside hydrolase family 77, GH77, which belongs to the alpha-amylase superfamily, Clan H, together with GH13 and GH70
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
this entry covers the former separate entry for EC 2.4.1.3. (amylomaltase). The plant enzyme has been termed D-enzyme. An enzymic activity of this nature forms part of the mammalian and yeast glycogen debranching system (see EC 3.2.1.33 amylo-1,6-glucosidase)
-
-
-
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
catalytic mechanism and domain structure and function
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reaction mechanism and catalytic cycle, the catalytic nucleophile changes conformation dramatically during the reaction, Gln256 on the 250s loop is involved in orienting the substrate in the +1 site. The absence of a suitable base in the covalent intermediate structure explains the low hydrolysis activity, overview
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
cyclization mechanism of amylomaltase, and large-ring cyclodextrin production by amylomaltase overview
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
cyclization mechanism of amylomaltase AtDPE1, overview
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
-
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
-
-
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
-
-
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
-
-
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
-
-
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
-
-
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
-
-
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
-
-
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
-
-
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
-
-
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
-
-
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
-
-
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
-
-
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
-
-
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
-
-
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
-
-
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
-
-
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
-
-
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
-
-
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
-
-
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
-
-
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
-
-
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
-
-
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
Pyrobaculum calidifontis DSM 21063
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-
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
-
-
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
Corynebacterium glutamicum CCUG 27702
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Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
Corynebacterium glutamicum NBRC 12168
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-
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
Corynebacterium glutamicum NRRL B-2784
-
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Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
-
-
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
Pyrobaculum aerophilum CIP 104966
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Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview
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Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
cyclization mechanism of amylomaltase, and large-ring cyclodextrin production by amylomaltase overview
Thermus aquaticus ATCC 33923
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
transglycosylation
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PATHWAY SOURCE
PATHWAYS
MetaCyc
glycogen degradation I, glycogen degradation II, starch degradation II, starch degradation V, sucrose biosynthesis II
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SYSTEMATIC NAME
IUBMB Comments
(1->4)-alpha-D-glucan:(1->4)-alpha-D-glucan 4-alpha-D-glycosyltransferase
This entry covers the former separate entry for EC 2.4.1.3 (amylomaltase). The plant enzyme has been termed D-enzyme. An enzymic activity of this nature forms part of the mammalian and yeast glycogen debranching system (see EC 3.2.1.33 amylo-alpha-1,6-glucosidase).
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CAS REGISTRY NUMBER
COMMENTARY
9032-09-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(alpha-1,4 glucan)m + (alpha-1,4 glucan)n
(alpha-1,4 glucan)m-x + (alpha-1,4 glucan)n+x
B7A9X4
Substrates: -
Products: -
Products: -
r
(alpha-1,4-D-glucan)m + (alpha-1,4-D-glucan)m
cyclic(alpha-1,4-glucan)x + (alpha-1,4-D-glucan)m-x
(alpha-1,4-D-glucan)m + (alpha-1,4-D-glucan)n
(alpha-1,4-D-glucan)m-x + (alpha-1,4-D-glucan)n+x
2-chloro-4-nitrophenyl 4'''',6''''-O-(3-oxobutylidene)maltopentaoside + D-glucose
?
-
Substrates: the disproportionation reaction of the enzyme involves a ping-pong bi-bi mechanism. On the basis of this reaction mechanism, the glycosyl-enzyme intermediate, in which a donor substrate is covalently bound to the catalytic nucleophile, is trapped by treating the enzyme with 3-ketobutylidene-beta-2-chloro-4-nitrophenyl maltopentaoside in the absence of an acceptor and is detected by matrix-assisted laser desorption ionization time-of-flight mass spectrometry after peptic digestion
Products: -
Products: -
?
6-O-alpha-D-glucosyl-cyclodextrins + H2O
D-glucose + cyclodextrins
-
Substrates: -
Products: -
Products: -
?
6-O-alpha-D-glucosyl-cyclomalto-octaose + H2O
D-glucose + cyclodextrins
-
Substrates: -
Products: -
Products: -
?
6-O-alpha-D-glucosyl-cyclomaltoheptaose + H2O
D-glucose + cyclodextrins
-
Substrates: -
Products: -
Products: -
?
64-O-alpha-maltooligosyl-pyridylamino-maltooctaose + maltohexaose
64-O-alpha-D-glucosyl-pyridylamino-maltooctaose + ?
-
Substrates: 4-alpha-glucanotransferase action of porcine liver GDE on four 64-O-alpha-maltooligosyl-pyridylamino-maltooctaoses, in the presence or absence of an acceptor, maltohexaose, overview
Products: -
Products: -
?
amylomaize V + glycosyl acceptor
cycloamylose + ?
-
Substrates: -
Products: -
Products: -
?
amylopectin + D-glucose
small oligosaccharides
Substrates: -
Products: without maltose
Products: without maltose
?
amylose
cycloamylose
-
Substrates: the enzyme produces a cycloamylose with a minimum degree of polymerization of 16
Products: -
Products: -
?
barley starch + glycosyl acceptor
?
-
Substrates: transgenic barley amylose-only starch which consists of more than 99% amylose
Products: -
Products: -
?
beta-cyclodextrin + mangiferin
glucosyl-alpha-(1->6)-mangiferin + maltosyl-alpha-(1->6)-mangiferin
cassava starch + glycosyl acceptor
?
-
Substrates: -
Products: -
Products: -
?
cassava starch + glycosyl acceptor
large ring-cyclodextrins 25-80
-
Substrates: -
Products: -
Products: -
?
cassava starch + glycosyl acceptor
large-ring cyclodextrins 24-29
-
Substrates: -
Products: -
Products: -
?
cassava starch + glycosyl acceptor
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
corn starch + glycosyl acceptor
?
Substrates: -
Products: -
Products: -
?
dodecyl-beta-maltoside + alpha-cyclodextrin
dodecyl-beta-maltooctaoside + ?
-
Substrates: -
Products: -
Products: -
?
dodecyl-beta-maltoside + starch
dodecyl-beta-maltooctaoside + ?
-
Substrates: when starch is used as glycosyl donor in the CGTase catalyzed alkyl glycoside elongation reaction, it is important to choose reaction conditions under which the cyclization of starch to alpha-cyclodextrin is efficient, since alpha-cyclodextrin may form low reactivity complexes with dodecyl-beta-maltoside
Products: -
Products: -
?
Glc-alpha-(1,4)-Glc-alpha-(1,4)-Glc-alpha(1,4)(Glc-alpha-(1,4)-Glc-alpha-(1,4)Glc-alpha-(1,4)-Glc-alpha-(1,6))Glc-alpha-(1,4)-Glc-alpha(1,4)-Glc-alpha-(1,4)-Glc-alpha-(1,4)-(1-deoxy-1-[(2-pyridyl)amino]-D-glucitol)
Glc-alpha-(1,4)-Glc-alpha-(1,4)-Glc-alpha-(1,4)(Glc-alpha-(1,6))Glc-alpha-(1,4)-Glc-alpha-(1,4)-Glc-alpha-(1,4)-Glc-alpha-(1,4)-(1-deoxy-1-[(2-pyridyl)amino]-D-glucitol) + Glc-alpha-(1,4)-Glc-alpha-(1,4)-Glc-alpha-(1,4)-Glc-alpha-(1,4)-Glc-alpha-(1,4)-Glc-alpha-(1,4)-Glc-alpha-(1,4)-(1-deoxy-1-[(2-pyridyl)amino]-D-glucitol)
-
Substrates: i.e. B5/84 + G6PA
Products: -
Products: -
?
Glcalpha(1,4)Glcalpha(1,4)Glcalpha(1,4)(Glcalpha(1,4)Glcalpha(1,4)Glcalpha(1,4)Glcalpha(1,6))Glcalpha(1,4)Glcalpha(1,4)Glcalpha(1,4)Glcalpha(1,4)Glc-pyridylamine + H2O
maltotriose + Glcalpha(1,4)Glcalpha(1,4)Glcalpha(1,4)(Glcalpha(1,6))Glcalpha(1,4)Glcalpha(1,4)Glcalpha(1,4)Glcalpha(1,4)Glc-pyridylamine
-
Substrates: -
Products: -
Products: -
?
glycogen + glycosyl acceptor
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
glycogen + maltooligosaccharides
D-glucose + ?
-
Substrates: -
Products: -
Products: -
?
maize starch + glycosyl acceptor
?
-
Substrates: 100% amylopectin waxy maize starch
Products: -
Products: -
?
maltodextrin + D-glucose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltodextrin + maltose
maltooligosaccharides + alpha-D-glucose
Substrates: -
Products: -
Products: -
?
maltoheptaose
maltodextrin + D-glucose
Substrates: -
Products: -
Products: -
?
maltoheptaose + glycosyl acceptor
maltose + D-glucose + maltooligosaccharides
-
Substrates: worst substrate
Products: -
Products: -
?
maltoheptaose + maltoheptaose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltoheptaose + maltotriose
maltononaose + D-glucose
-
Substrates: D-enzyme
Products: -
Products: -
?
maltohexaose + maltohexaose
maltooligosaccharide
-
Substrates: -
Products: -
Products: -
?
maltohexaose + maltohexaose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltohexaose + maltotriose
D-glucose + maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltononaose + maltotriose
maltoundecaose + D-glucose
-
Substrates: D-enzyme
Products: -
Products: -
?
maltooligosaccharides
maltooligosaccharides + D-glucose
-
Substrates: -
Products: -
Products: -
?
maltopentaose + maltotriose
homologous 1,4-alpha-D-glucans
-
Substrates: amylomaltose
Products: -
Products: -
?
maltopentaose + maltotriose
maltoheptaose + D-glucose
-
Substrates: D-enzyme
Products: -
Products: -
?
maltose + D-glucose
maltodextrin + D-glucose
Substrates: -
Products: -
Products: -
?
maltose + glycosyl acceptor
D-glucose
Substrates: efficient transglycosylation activity
Products: -
Products: -
?
maltose + maltose
maltooligosaccharides + D-glucose
Substrates: -
Products: -
Products: -
?
maltosyl-alpha-(1->6)-puerarin
?
-
Substrates: i.e. maltosyl-daidzein 8-C-glucoside
Products: combined action of maltogenic amylase reactions from Bacillus stearothermophilus and 4-alpha-glucanotransferase from Thermus scotoductus increases the water solubility of puerarin, an isoflavonoid derived from Radix puerariae
Products: combined action of maltogenic amylase reactions from Bacillus stearothermophilus and 4-alpha-glucanotransferase from Thermus scotoductus increases the water solubility of puerarin, an isoflavonoid derived from Radix puerariae
?
maltotetraose + maltotriose
glucose + maltoheptaose + maltodecaose
-
Substrates: D-enzyme
Products: -
Products: -
?
maltotetraose + maltotriose
homologous 1,4-alpha-glucans
-
Substrates: amylomaltose
Products: -
Products: -
?
maltotheptaose + maltotriose
D-glucose + maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltotriose
maltodextrin + D-glucose
Substrates: -
Products: -
Products: -
?
maltotriose + glycosyl acceptor
D-glucose + maltose + maltotetraose + maltopentaose + maltohexaose
-
Substrates: -
Products: -
Products: -
?
maltotriose + maltotriose
D-glucose + maltopentaose + maltoheptaose + maltononaose + maltoundecaose
-
Substrates: D-enzyme
Products: -
Products: -
?
maltotriose + maltotriose
homologous alpha-1,4-D-glucans
-
Substrates: amylomaltose
Products: -
Products: -
?
maltotriose + maltotriose
maltooligosaccharides + D-glucose
Substrates: -
Products: -
Products: -
?
pea starch + glycosyl acceptor
cycloamylose + ?
Substrates: -
Products: -
Products: -
?
pea starch + glycosyl acceptor
large ring-cyclodextrins 23-26
-
Substrates: -
Products: -
Products: -
?
pea starch + glycosyl acceptor
large ring-cyclodextrins 29-33
-
Substrates: -
Products: -
Products: -
?
pea starch + glycosyl acceptor
large-ring cyclodextrins 24-29
-
Substrates: -
Products: -
Products: -
?
potato amylose + glycosyl acceptor
cycloamylose + ?
-
Substrates: -
Products: -
Products: -
?
potato starch + glycosyl acceptor
?
Substrates: -
Products: -
Products: -
?
starch + erythritol
maltotriosyl-erythritol + ?
-
Substrates: maltotriosyl-erythritol (EG3) is synthesized via transglycosylation by recombinant amylomaltase (AMase), tapioca starch serves as the glucosyl donor, and erythritol as the acceptor. HPLC analysis reveals an EG3 yield of 14.0% with a concentration of 2.8 mg/ml. Mass spectrometry confirms the molecular weight of EG3 as 608 Da, and its structure is verified by 1H and 13C NMR analysis. Starch transglycosylation assay
Products: -
Products: -
?
starch + glycosyl acceptor
D-glucose + maltose + glucan oligosaccharides
-
Substrates: -
Products: -
Products: -
?
starch + N-acetyl-D-glucosamine
oligosaccharides terminated by 4-O-alpha-D-glucopyranosyl-N-acetyl-D-glucosamine
(alpha-1,4-D-glucan)m + (alpha-1,4-D-glucan)m
cyclic(alpha-1,4-glucan)x + (alpha-1,4-D-glucan)m-x
-
Substrates: -
Products: -
Products: -
r
(alpha-1,4-D-glucan)m + (alpha-1,4-D-glucan)m
cyclic(alpha-1,4-glucan)x + (alpha-1,4-D-glucan)m-x
-
Substrates: -
Products: -
Products: -
r
(alpha-1,4-D-glucan)m + (alpha-1,4-D-glucan)n
(alpha-1,4-D-glucan)m-x + (alpha-1,4-D-glucan)n+x
-
Substrates: -
Products: -
Products: -
r
(alpha-1,4-D-glucan)m + (alpha-1,4-D-glucan)n
(alpha-1,4-D-glucan)m-x + (alpha-1,4-D-glucan)n+x
-
Substrates: -
Products: -
Products: -
r
(alpha-1,4-D-glucan)m + H2O
(alpha-1,4-D-glucan)x + (alpha-1,4-D-glucan)m-x
-
Substrates: -
Products: -
Products: -
r
(alpha-1,4-D-glucan)m + H2O
(alpha-1,4-D-glucan)x + (alpha-1,4-D-glucan)m-x
-
Substrates: -
Products: -
Products: -
r
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharide
Substrates: -
Products: -
Products: -
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharide
-
Substrates: maltose and a highly branched, soluble heteroglycan are excellent substrates for DPE2
Products: -
Products: -
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
Substrates: it is proposed that a soluble heteroglycan is the in vivo substrate for DPE2. An alternative route to metabolize the glucan residues in soluble heteroglycane exists in Arabidopsis thaliana
Products: -
Products: -
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
-
Substrates: it is proposed that a soluble heteroglycan is the in vivo substrate for DPE2. An alternative route to metabolize the glucan residues in soluble heteroglycan exists in Escherichia coli
Products: -
Products: -
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
Substrates: -
Products: -
Products: -
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
B7A9X4
Substrates: -
Products: -
Products: -
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
1,4-alpha-D-glucan + glucose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
1,4-alpha-D-glucan + glucose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
1,4-alpha-D-glucan + glucose
maltooligosaccharides
Substrates: -
Products: -
Products: -
?
1,4-alpha-D-glucan + glucose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
1,4-alpha-D-glucan + glucose
maltooligosaccharides
B7A9X4
Substrates: -
Products: -
Products: -
?
1,4-alpha-D-glucan + glucose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
amylopectin
?
Substrates: incubation of the enzyme with starch or its constituents, i.e. amylose and amylopectin, leads to the formation of a set of multiples of maltose (i.e. maltose, maltotetraose, maltohexaose etc.)
Products: -
Products: -
?
amylopectin
?
Substrates: incubation of the enzyme with starch or its constituents, i.e. amylose and amylopectin, leads to the formation of a set of multiples of maltose (i.e. maltose, maltotetraose, maltohexaose etc.)
Products: -
Products: -
?
amylopectin + maltopentaose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
amylopectin + maltopentaose
maltooligosaccharides
Substrates: -
Products: -
Products: -
?
amylopectin + maltopentaose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
amylopectin + maltopentaose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
amylopectin + maltopentaose
maltooligosaccharides
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
Substrates: -
Products: -
Products: -
?
amylopectin + maltopentaose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
amylose
?
Substrates: incubation of the enzyme with starch or its constituents, i.e. amylose and amylopectin, leads to the formation of a set of multiples of maltose (i.e. maltose, maltotetraose, maltohexaose etc.)
Products: -
Products: -
?
amylose
?
Substrates: incubation of the enzyme with starch or its constituents, i.e. amylose and amylopectin, leads to the formation of a set of multiples of maltose (i.e. maltose, maltotetraose, maltohexaose etc.)
Products: -
Products: -
?
amylose + D-glucose
low molecular mass oligosaccharides
Substrates: -
Products: -
Products: -
?
amylose + D-glucose
low molecular mass oligosaccharides
-
Substrates: -
Products: -
Products: -
?
amylose + D-glucose
low molecular mass oligosaccharides
-
Substrates: synthetic amylose AS-320
Products: -
Products: -
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
-
Substrates: -
Products: cycloamylose
Products: cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
Substrates: -
Products: -
Products: -
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
-
Substrates: -
Products: -
Products: -
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
-
Substrates: -
Products: cycloamylose
Products: cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
Substrates: -
Products: cycloamylose
Products: cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
B7A9X4
Substrates: -
Products: cycloamylose
Products: cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
-
Substrates: -
Products: cycloamylose
Products: cycloamylose
?
amylose + maltopentaose
maltooligosaccharides
Substrates: -
Products: -
Products: -
?
amylose + maltopentaose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
amylose + maltopentaose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
beta-cyclodextrin + mangiferin
glucosyl-alpha-(1->6)-mangiferin + maltosyl-alpha-(1->6)-mangiferin
Substrates: -
Products: -
Products: -
?
beta-cyclodextrin + mangiferin
glucosyl-alpha-(1->6)-mangiferin + maltosyl-alpha-(1->6)-mangiferin
Parageobacillus galactosidasius DSM 18751
Substrates: -
Products: -
Products: -
?
beta-cyclodextrin + puerarin
?
Substrates: -
Products: -
Products: -
?
beta-cyclodextrin + puerarin
?
Parageobacillus galactosidasius DSM 18751
Substrates: -
Products: -
Products: -
?
corn starch + glycosyl acceptor
large-ring cyclodextrins
-
Substrates: -
Products: -
Products: -
?
corn starch + glycosyl acceptor
large-ring cyclodextrins
-
Substrates: -
Products: -
Products: -
?
glutinous-rice starch + glycosyl acceptor
large-ring cyclodextrins
-
Substrates: -
Products: -
Products: -
?
glutinous-rice starch + glycosyl acceptor
large-ring cyclodextrins
-
Substrates: -
Products: -
Products: -
?
linear maltooligosaccharides + starch
?
Substrates: -
Products: -
Products: -
r
linear maltooligosaccharides + starch
?
-
Substrates: -
Products: -
Products: -
r
maltodextrin + maltodextrin
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltodextrin + maltodextrin
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltodextrin + maltodextrin
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltodextrin + maltose
maltooligosaccharides
-
Substrates: catabolic processing of glycogen and maltodextrins
Products: -
Products: -
?
maltodextrin + maltose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltodextrin + maltose
maltooligosaccharides
Substrates: -
Products: -
Products: -
?
maltodextrin + maltose
maltooligosaccharides
-
Substrates: catabolic processing of glycogen and maltodextrins
Products: -
Products: -
?
maltodextrin + maltose
maltooligosaccharides
-
Substrates: catabolic processing of glycogen and maltodextrins
Products: -
Products: -
?
maltoheptaose + maltoheptaose
?
-
Substrates: -
Products: -
Products: -
?
maltoheptaose + maltoheptaose
?
Substrates: chain length distribution of the transfer products ranges from DP2 to about DP20, which is the upper size limit of oligosaccharides resolved with the TLC system used, but presumably even larger oligomers are also formed. Glucose is not observed as a product. The transfer products exclusively contain 1,4-glucosidic linkages
Products: -
Products: -
?
maltoheptaose + maltoheptaose
?
Substrates: chain length distribution of the transfer products ranges from DP2 to about DP20, which is the upper size limit of oligosaccharides resolved with the TLC system used, but presumably even larger oligomers are also formed. Glucose is not observed as a product. The transfer products exclusively contain 1,4-glucosidic linkages
Products: -
Products: -
?
maltoheptaose + maltoheptaose
D-glucose + maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltoheptaose + maltoheptaose
D-glucose + maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltoheptaose + maltopentaose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltoheptaose + maltopentaose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltoheptaose + maltopentaose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltoheptaose + maltopentaose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltoheptaose + maltopentaose
maltooligosaccharides
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
Substrates: -
Products: -
Products: -
?
maltohexaose + glycosyl acceptor
maltose + D-glucose + maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltohexaose + glycosyl acceptor
maltose + D-glucose + maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltohexaose + maltodextrin
D-glucose + maltopentaose
-
Substrates: only amylomaltase, no polymers larger than the initial maltodextrin substrate, maltohexaose is a good donor substrate, but unable to function as an acceptor
Products: -
Products: -
?
maltohexaose + maltodextrin
D-glucose + maltopentaose
Stutzerimonas stutzeri NRRL B3389
-
Substrates: only amylomaltase, no polymers larger than the initial maltodextrin substrate, maltohexaose is a good donor substrate, but unable to function as an acceptor
Products: -
Products: -
?
maltohexaose + maltohexaose
?
Substrates: chain length distribution of the transfer products ranges from DP2 to about DP20, which is the upper size limit of oligosaccharides resolved with the TLC system used, but presumably even larger oligomers are also formed. Glucose is not observed as a product. The transfer products exclusively contain 1,4-glucosidic linkages
Products: -
Products: -
?
maltohexaose + maltohexaose
?
Substrates: chain length distribution of the transfer products ranges from DP2 to about DP20, which is the upper size limit of oligosaccharides resolved with the TLC system used, but presumably even larger oligomers are also formed. Glucose is not observed as a product. The transfer products exclusively contain 1,4-glucosidic linkages
Products: -
Products: -
?
maltohexaose + maltohexaose
D-glucose + maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltohexaose + maltohexaose
D-glucose + maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltohexaose + maltopentaose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltohexaose + maltopentaose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltohexaose + maltopentaose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltohexaose + maltopentaose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltohexaose + maltopentaose
maltooligosaccharides
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
Substrates: -
Products: -
Products: -
?
maltohexaose + maltotriose
maltodextrins
-
Substrates: -
Products: -
Products: -
?
maltopentaose + glycosyl acceptor
maltose + D-glucose + maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltopentaose + glycosyl acceptor
maltose + D-glucose + maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltopentaose + maltodextrin
maltose + higher dextrins
-
Substrates: -
Products: -
Products: -
?
maltopentaose + maltodextrin
maltose + higher dextrins
Stutzerimonas stutzeri NRRL B3389
-
Substrates: -
Products: -
Products: -
?
maltopentaose + maltopentaose
?
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Substrates: -
Products: -
Products: -
?
maltopentaose + maltopentaose
D-glucose + maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltopentaose + maltopentaose
D-glucose + maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltopentaose + maltopentaose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltopentaose + maltopentaose
maltooligosaccharides
-
Substrates: metabolism of starch in the bacterium
Products: -
Products: -
?
maltopentaose + maltopentaose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltopentaose + maltopentaose
maltooligosaccharides
-
Substrates: metabolism of starch in the bacterium
Products: -
Products: -
?
maltopentaose + maltopentaose
maltooligosaccharides
-
Substrates: metabolism of starch in the bacterium
Products: -
Products: -
?
maltopentaose + maltopentaose
maltooligosaccharides
-
Substrates: metabolism of starch in the bacterium
Products: -
Products: -
?
maltopentaose + maltopentaose
maltooligosaccharides
-
Substrates: metabolism of starch in the bacterium
Products: -
Products: -
?
maltopentaose + maltopentaose
maltooligosaccharides
-
Substrates: metabolism of starch in the bacterium
Products: -
Products: -
?
maltopentaose + maltopentaose
maltooligosaccharides
Stutzerimonas stutzeri NRRL B3389
-
Substrates: metabolism of starch in the bacterium
Products: -
Products: -
?
maltopentaose + maltopentaose
maltooligosaccharides
-
Substrates: metabolism of starch in the bacterium
Products: -
Products: -
?
maltopentaose + maltopentaose
maltooligosaccharides
-
Substrates: metabolism of starch in the bacterium
Products: -
Products: -
?
maltopentaose + maltopentaose
new oligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltopentaose + maltopentaose
new oligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltopentaose + maltopentaose
new oligosaccharides
-
Substrates: capable of transferring segments of 2 to 5 glucose residues linked by alpha-D-1-4 linkages from maltopentaose, higher molecular weight maltohomologues and starch to maltopentaose and other maltooligosaccharides
Products: -
Products: -
?
maltopentaose + maltopentaose
new oligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltopentaose + maltopentaose
new oligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltopentaose + maltopentaose
new oligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltopentaose + maltotriose
D-glucose + maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltopentaose + maltotriose
D-glucose + maltooligosaccharides
Substrates: -
Products: -
Products: -
?
maltose + (1,4-alpha-glucan)n+1
D-glucose + (1,4-alpha-glucan)n+1
-
Substrates: -
Products: -
Products: -
?
maltose + (1,4-alpha-glucan)n+1
D-glucose + (1,4-alpha-glucan)n+1
-
Substrates: -
Products: -
Products: -
?
maltose + beta-cyclodextrin
6-O-alpha-maltosyl-beta-cyclodextrin
-
Substrates: condensation reaction mechanism, overview
Products: mass spectrometric product identification
Products: mass spectrometric product identification
?
maltose + beta-cyclodextrin
6-O-alpha-maltosyl-beta-cyclodextrin
-
Substrates: condensation reaction mechanism, overview
Products: mass spectrometric product identification
Products: mass spectrometric product identification
?
maltose + glycosyl acceptor
?
-
Substrates: lowest activity
Products: -
Products: -
?
maltose + glycosyl acceptor
?
-
Substrates: lowest activity
Products: -
Products: -
?
maltose + maltose
?
-
Substrates: worst substrate
Products: -
Products: -
?
maltose + maltose
maltooligosaccharides
Substrates: -
Products: -
Products: -
?
maltose + maltose
maltotriose + glucose
-
Substrates: -
Products: -
Products: -
?
maltose + maltose
maltotriose + glucose
-
Substrates: D-enzyme
Products: -
Products: -
?
maltose + maltose
maltotriose + glucose
Substrates: key role in maltose metabolism
Products: -
Products: -
?
maltose + maltosyl-beta-cyclodextrin
?
-
Substrates: -
Products: -
Products: -
?
maltose + maltosyl-beta-cyclodextrin
?
-
Substrates: -
Products: -
Products: -
?
maltotetraose + glycosyl acceptor
maltose + D-glucose + maltooligosaccharides
-
Substrates: second best substrate
Products: -
Products: -
?
maltotetraose + glycosyl acceptor
maltose + D-glucose + maltooligosaccharides
-
Substrates: second best substrate
Products: -
Products: -
?
maltotetraose + maltodextrin
maltose + higher dextrins
-
Substrates: -
Products: -
Products: -
?
maltotetraose + maltodextrin
maltose + higher dextrins
Stutzerimonas stutzeri NRRL B3389
-
Substrates: -
Products: -
Products: -
?
maltotetraose + maltopentaose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltotetraose + maltopentaose
maltooligosaccharides
Substrates: -
Products: -
Products: -
?
maltotetraose + maltopentaose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltotetraose + maltopentaose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltotetraose + maltopentaose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltotetraose + maltopentaose
maltooligosaccharides
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
Substrates: -
Products: -
Products: -
?
maltotetraose + maltotetraose
?
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Substrates: -
Products: -
Products: -
?
maltotetraose + maltotetraose
D-glucose + maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltotetraose + maltotetraose
D-glucose + maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltotetraose + maltotetraose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltotetraose + maltotetraose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltotetraose + maltotriose
D-glucose + maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltotetraose + maltotriose
D-glucose + maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltotetraose + maltotriose
D-glucose + maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltotetraose + maltotriose
D-glucose + maltooligosaccharides
Substrates: -
Products: -
Products: -
?
maltotetraose + maltotriose
D-glucose + maltooligosaccharides
-
Substrates: amylomaltose, most active with maltotetraose
Products: -
Products: -
?
maltotetraose + maltotriose
maltodextrins
Substrates: -
Products: -
Products: -
?
maltotheptaose + maltotriose
maltodextrins
-
Substrates: -
Products: -
Products: -
?
maltotriose + glycosyl acceptor
D-glucose + maltooligosaccharides
Substrates: efficient transglycosylation activity
Products: -
Products: -
?
maltotriose + glycosyl acceptor
D-glucose + maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltotriose + glycosyl acceptor
maltose + D-glucose + maltooligosaccharides
Substrates: the wild type enzyme prefers maltotriose for disproportionation reaction
Products: -
Products: -
?
maltotriose + glycosyl acceptor
maltose + D-glucose + maltooligosaccharides
-
Substrates: best substrate
Products: -
Products: -
?
maltotriose + glycosyl acceptor
maltose + D-glucose + maltooligosaccharides
-
Substrates: best substrate
Products: -
Products: -
?
maltotriose + glycosyl acceptor
maltose + D-glucose + maltooligosaccharides
Substrates: the wild type enzyme prefers maltotriose for disproportionation reaction
Products: -
Products: -
?
maltotriose + maltodextrin
maltopentaose + ?
-
Substrates: amylomaltase
Products: -
Products: -
?
maltotriose + maltodextrin
maltopentaose + ?
Stutzerimonas stutzeri NRRL B3389
-
Substrates: amylomaltase
Products: -
Products: -
?
maltotriose + maltodextrin
maltose + higher dextrins
-
Substrates: -
Products: -
Products: -
?
maltotriose + maltodextrin
maltose + higher dextrins
Stutzerimonas stutzeri NRRL B3389
-
Substrates: -
Products: -
Products: -
?
maltotriose + maltotriose
D-glucose + maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltotriose + maltotriose
D-glucose + maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltotriose + maltotriose
D-glucose + maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltotriose + maltotriose
D-glucose + maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltotriose + maltotriose
D-glucose + maltopentaose
-
Substrates: -
Products: -
Products: -
?
maltotriose + maltotriose
D-glucose + maltopentaose
-
Substrates: -
Products: -
Products: -
?
maltotriose + maltotriose
glucose + maltooligosaccharides
Substrates: -
Products: -
Products: -
?
maltotriose + maltotriose
glucose + maltooligosaccharides
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Substrates: -
Products: -
Products: -
?
maltotriose + maltotriose
maltodextrins
-
Substrates: -
Products: -
Products: -
?
maltotriose + maltotriose
maltodextrins
-
Substrates: Mtase
Products: -
Products: -
?
maltotriose + maltotriose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltotriose + maltotriose
maltooligosaccharides
Substrates: -
Products: -
Products: -
?
maltotriose + maltotriose
maltooligosaccharides
-
Substrates: most efficient substrate
Products: -
Products: -
?
maltotriose + maltotriose
maltooligosaccharides
Substrates: -
Products: -
Products: -
?
maltotriose + maltotriose
maltooligosaccharides
-
Substrates: most efficient substrate
Products: -
Products: -
?
maltotriose + maltotriose
maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltotriose + maltotriose
maltopentaose + D-glucose
-
Substrates: -
Products: -
Products: -
?
maltotriose + maltotriose
maltopentaose + D-glucose
-
Substrates: -
Products: -
Products: -
?
maltotriose + maltotriose
maltopentaose + D-glucose
-
Substrates: -
Products: -
Products: -
?
maltotriose + maltotriose
maltopentaose + D-glucose
-
Substrates: D-enzyme
Products: -
Products: -
?
maltotriose + maltotriose
maltopentaose + maltotetraose
-
Substrates: -
Products: -
Products: -
?
maltotriose + maltotriose
maltopentaose + maltotetraose
-
Substrates: -
Products: -
Products: -
?
maltotriose + maltotriose
maltopentaose + maltotetraose
-
Substrates: -
Products: -
Products: -
?
maltotriose + maltotriose
maltopentaose + maltotetraose
-
Substrates: -
Products: -
Products: -
?
pea starch + glycosyl acceptor
?
-
Substrates: -
Products: -
Products: -
?
pea starch + glycosyl acceptor
large-ring cyclodextrins
-
Substrates: -
Products: -
Products: -
?
pea starch + glycosyl acceptor
large-ring cyclodextrins
Substrates: -
Products: -
Products: -
?
pea starch + glycosyl acceptor
large-ring cyclodextrins
Substrates: -
Products: -
Products: -
?
potato amylose + glycosyl acceptor
cycloamylose
Substrates: -
Products: the enzyme can produce cycloamyloses in the range 1650 glucose residues
Products: the enzyme can produce cycloamyloses in the range 1650 glucose residues
?
potato amylose + glycosyl acceptor
cycloamylose
-
Substrates: -
Products: the enzyme can produce cycloamyloses in the range 16 to more than 60 glucose residues
Products: the enzyme can produce cycloamyloses in the range 16 to more than 60 glucose residues
?
potato starch + maltose
large-ring cyclodextrins
-
Substrates: -
Products: -
Products: -
?
potato starch + maltose
large-ring cyclodextrins
-
Substrates: -
Products: -
Products: -
?
rice starch + glycosyl acceptor
large-ring cyclodextrins
-
Substrates: -
Products: -
Products: -
?
rice starch + glycosyl acceptor
large-ring cyclodextrins
-
Substrates: -
Products: -
Products: -
?
soluble potato starch + glycosyl acceptor
?
-
Substrates: -
Products: -
Products: -
?
soluble potato starch + glycosyl acceptor
?
-
Substrates: -
Products: -
Products: -
?
starch
?
Substrates: incubation of the enzyme with starch or its constituents, i.e. amylose and amylopectin, leads to the formation of a set of multiples of maltose (i.e. maltose, maltotetraose, maltohexaose etc.)
Products: -
Products: -
?
starch
?
Substrates: incubation of the enzyme with starch or its constituents, i.e. amylose and amylopectin, leads to the formation of a set of multiples of maltose (i.e. maltose, maltotetraose, maltohexaose etc.)
Products: -
Products: -
?
starch + D-allose
oligosaccharides terminated by 4-O-alpha-D-glucopyranosyl-D-allose
-
Substrates: -
Products: -
Products: -
?
starch + D-allose
oligosaccharides terminated by 4-O-alpha-D-glucopyranosyl-D-allose
-
Substrates: -
Products: -
Products: -
?
starch + D-allose
oligosaccharides terminated by 4-O-alpha-D-glucopyranosyl-D-allose
-
Substrates: -
Products: -
Products: -
?
starch + D-glucose
low molecular mass oligosaccharides
Substrates: -
Products: -
Products: -
?
starch + D-glucose
low molecular mass oligosaccharides
-
Substrates: -
Products: -
Products: -
?
starch + D-glucose
low molecular mass oligosaccharides
-
Substrates: soluble starch
Products: -
Products: -
?
starch + D-mannose
oligosaccharides terminated by 4-O-alpha-D-glucopyranosyl-D-mannose
-
Substrates: -
Products: -
Products: -
?
starch + D-mannose
oligosaccharides terminated by 4-O-alpha-D-glucopyranosyl-D-mannose
-
Substrates: -
Products: -
Products: -
?
starch + D-mannose
oligosaccharides terminated by 4-O-alpha-D-glucopyranosyl-D-mannose
-
Substrates: -
Products: -
Products: -
?
starch + D-xylose
oligosaccharides terminated by 4-O-alpha-D-glucopyranosyl-D-xylose
-
Substrates: -
Products: -
Products: -
?
starch + D-xylose
oligosaccharides terminated by 4-O-alpha-D-glucopyranosyl-D-xylose
-
Substrates: -
Products: -
Products: -
?
starch + D-xylose
oligosaccharides terminated by 4-O-alpha-D-glucopyranosyl-D-xylose
-
Substrates: -
Products: -
Products: -
?
starch + maltohexaose
?
Substrates: -
Products: -
Products: -
?
starch + maltohexaose
?
Substrates: -
Products: -
Products: -
?
starch + maltohexaose
?
Substrates: -
Products: -
Products: -
?
starch + maltohexaose
?
Substrates: -
Products: -
Products: -
?
starch + maltohexaose
?
Substrates: -
Products: -
Products: -
?
starch + maltohexaose
?
Substrates: -
Products: -
Products: -
?
starch + maltopentaose
?
Substrates: -
Products: -
Products: -
?
starch + maltopentaose
?
Substrates: -
Products: -
Products: -
?
starch + maltopentaose
?
Substrates: -
Products: -
Products: -
?
starch + maltopentaose
?
Substrates: -
Products: -
Products: -
?
starch + maltopentaose
?
Substrates: -
Products: -
Products: -
?
starch + maltopentaose
?
Substrates: -
Products: -
Products: -
?
starch + maltopentaose
alpha-1,4-D-glucans
-
Substrates: -
Products: -
Products: -
?
starch + maltopentaose
alpha-1,4-D-glucans
Substrates: -
Products: -
Products: -
?
starch + maltopentaose
alpha-1,4-D-glucans
-
Substrates: starch can serve as acceptor molecule in glycosyl transfer reactions
Products: -
Products: -
?
starch + maltopentaose
alpha-1,4-D-glucans
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
Substrates: starch can serve as acceptor molecule in glycosyl transfer reactions
Products: -
Products: -
?
starch + maltopentaose
alpha-1,4-D-glucans
-
Substrates: -
Products: -
Products: -
?
starch + maltotetraose
?
Substrates: -
Products: -
Products: -
?
starch + maltotetraose
?
Substrates: -
Products: -
Products: -
?
starch + maltotetraose
?
Substrates: -
Products: -
Products: -
?
starch + maltotetraose
?
Substrates: -
Products: -
Products: -
?
starch + maltotetraose
?
Substrates: -
Products: -
Products: -
?
starch + maltotetraose
?
Substrates: -
Products: -
Products: -
?
starch + maltotriose
?
Substrates: -
Products: -
Products: -
?
starch + maltotriose
?
Substrates: -
Products: -
Products: -
?
starch + maltotriose
?
Substrates: -
Products: -
Products: -
?
starch + maltotriose
?
Substrates: -
Products: -
Products: -
?
starch + maltotriose
?
Substrates: -
Products: -
Products: -
?
starch + maltotriose
?
Substrates: -
Products: -
Products: -
?
starch + N-acetyl-D-glucosamine
oligosaccharides terminated by 4-O-alpha-D-glucopyranosyl-N-acetyl-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
starch + N-acetyl-D-glucosamine
oligosaccharides terminated by 4-O-alpha-D-glucopyranosyl-N-acetyl-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
starch + N-acetyl-D-glucosamine
oligosaccharides terminated by 4-O-alpha-D-glucopyranosyl-N-acetyl-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
tapioca starch + glycosyl acceptor
large-ring cyclodextrins
-
Substrates: -
Products: -
Products: -
?
tapioca starch + glycosyl acceptor
large-ring cyclodextrins
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
Products: -
Products: -
-
additional information
?
-
Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
Products: -
Products: -
-
additional information
?
-
Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
Products: -
Products: -
-
additional information
?
-
Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
Products: -
Products: -
-
additional information
?
-
-
Substrates: the smallest acceptor is glucose, the smallest donor is maltose
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme produces oligosaccharides with degree of polymerization (DP) of DP16-DP50 from amylose
Products: -
Products: -
-
additional information
?
-
Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Highest catalytic efficiency is found for maltopentaose, with decreasing values for all the other substrates, products have a degree of polymerization between 16 and 50
Products: -
Products: -
-
additional information
?
-
-
Substrates: 2 major forms, D1 and D2
Products: -
Products: -
?
additional information
?
-
-
Substrates: glucose is the major product of the D-enzyme reaction
Products: -
Products: -
?
additional information
?
-
-
Substrates: glucose is the major product of the D-enzyme reaction
Products: -
Products: -
?
additional information
?
-
-
Substrates: amylopectin is no substrate, maltose is not a product
Products: -
Products: -
?
additional information
?
-
-
Substrates: amylomaltase is involved in the conversion of maltose to sucrose in the cytosol
Products: -
Products: -
?
additional information
?
-
Substrates: 4-alpha-glucanotransferase is essential for maltose metabolism in photosynthetic leaves
Products: -
Products: -
?
additional information
?
-
Substrates: DPE2 transfers the non-reducing glucosyl unit from maltose to glycogen by a ping-pong mechanism. The forward reaction, i.e. consumption of maltose, is specific for the beta-anomer of maltose, while the reverse reaction, i.e. production of maltose, is not stereospecific for the acceptor glucose
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme AtDPE1 produces oligosaccharides with degree of polymerization (DP) of DP16-DP50 from potato amylose
Products: -
Products: -
-
additional information
?
-
Substrates: the enzyme AtDPE1 produces oligosaccharides with degree of polymerization (DP) of DP16-DP50 from potato amylose
Products: -
Products: -
-
additional information
?
-
-
Substrates: both isozymes AgtA and AgtB show transglycosylation activity on donor substrates with alpha-(1,4)-glycosidic bonds and at least five anhydroglucose units forming alpha-(1,4)-glycosidic bonds. Their reaction products reach a degree of polymerization of at least 30. Maltose and larger maltooligosaccharides are the most efficient acceptor substrates, although AgtA also uses small nigerooligosaccharides containing alpha-(1,3)-glycosidic bonds as acceptor substrate, reaction products, overview. The enzyme also shows hydrolyzing activity with potato starch
Products: -
Products: -
?
additional information
?
-
-
Substrates: glucose, maltose, maltotriose and maltotetraose are not acceptor molecules
Products: -
Products: -
?
additional information
?
-
-
Substrates: does not use maltose, maltotriose or maltotetraose as acceptor substrates in maltodextrinyltransfer reactions
Products: -
Products: -
?
additional information
?
-
Substrates: MalQ is able to hydrolyse malto-oligosaccharides as well as to form their longer transglycosylation products and shows activity towards glucose, G1, and a series of malto-oligosaccharides, G2-G7, i.e. maltose, maltotriose, maltotetraose, maltopentaose, maltohexaose and maltoheptaose
Products: -
Products: -
?
additional information
?
-
-
Substrates: MalQ is able to hydrolyse malto-oligosaccharides as well as to form their longer transglycosylation products and shows activity towards glucose, G1, and a series of malto-oligosaccharides, G2-G7, i.e. maltose, maltotriose, maltotetraose, maltopentaose, maltohexaose and maltoheptaose
Products: -
Products: -
?
additional information
?
-
-
Substrates: maltose is not a product
Products: -
Products: -
?
additional information
?
-
-
Substrates: glucose, maltose and maltotriose can act as acceptor, only maltotriose can act as donor
Products: -
Products: -
?
additional information
?
-
-
Substrates: glucose, maltose and maltotriose can act as acceptor, only maltotriose can act as donor
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme performs starch transglycosylation, starch degradation, disproportionation, hydrolysis, cyclization and coupling activities. The substrate specificity of wild-type and mutant enzymes for disproportionation activity is determined with malto-oligosaccharides (maltose (G2) to maltoheptaose (G7)), overview. The reaction products are analyzed by high-performance anion-exchange chromatography-pulsed amperometric detection (HPAEC-PAD)
Products: -
Products: -
-
additional information
?
-
Substrates: the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch
Products: -
Products: -
-
additional information
?
-
Substrates: maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview
Products: -
Products: -
-
additional information
?
-
Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
Products: -
Products: -
-
additional information
?
-
Substrates: the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch
Products: -
Products: -
-
additional information
?
-
Substrates: maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview
Products: -
Products: -
-
additional information
?
-
Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
Products: -
Products: -
-
additional information
?
-
Substrates: the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch
Products: -
Products: -
-
additional information
?
-
Substrates: maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview
Products: -
Products: -
-
additional information
?
-
Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
Products: -
Products: -
-
additional information
?
-
Substrates: the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch
Products: -
Products: -
-
additional information
?
-
Substrates: maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview
Products: -
Products: -
-
additional information
?
-
Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
Products: -
Products: -
-
additional information
?
-
Corynebacterium glutamicum CCUG 27702
Substrates: the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch
Products: -
Products: -
-
additional information
?
-
Corynebacterium glutamicum CCUG 27702
Substrates: maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview
Products: -
Products: -
-
additional information
?
-
Corynebacterium glutamicum CCUG 27702
Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
Products: -
Products: -
-
additional information
?
-
Substrates: the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch
Products: -
Products: -
-
additional information
?
-
Substrates: maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview
Products: -
Products: -
-
additional information
?
-
Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
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additional information
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Substrates: the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch
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additional information
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Substrates: maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
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additional information
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Substrates: the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch
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additional information
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Substrates: maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
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additional information
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Corynebacterium glutamicum NBRC 12168
Substrates: the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch
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additional information
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Corynebacterium glutamicum NBRC 12168
Substrates: maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview
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additional information
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Corynebacterium glutamicum NBRC 12168
Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
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additional information
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Substrates: the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch
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additional information
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Substrates: maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
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additional information
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Corynebacterium glutamicum NRRL B-2784
Substrates: the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch
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additional information
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Corynebacterium glutamicum NRRL B-2784
Substrates: maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview
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additional information
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Corynebacterium glutamicum NRRL B-2784
Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
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additional information
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Substrates: the enzyme displays weak hydrolytic activity against sucrose and alpha-aryl glucoside and fails to act on trehalose and isomaltose
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additional information
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Substrates: the enzyme displays weak hydrolytic activity against sucrose and alpha-aryl glucoside and fails to act on trehalose and isomaltose
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additional information
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Substrates: glucose is the major product of the D-enzyme reaction
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Synthesis of cycloamyloses (CAs) of small dimensions (DP of 5 and 7) is described for amylomaltase from the thermophilic bacterium Deinococcus geothermalis using as substrate the debranched products of amylomaize, instead of the usually used potato amylose or rice amylose
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Synthesis of cycloamyloses (CAs) of small dimensions (DP of 5 and 7) is described for amylomaltase from the thermophilic bacterium Deinococcus geothermalis using as substrate the debranched products of amylomaize, instead of the usually used potato amylose or rice amylose
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Synthesis of cycloamyloses (CAs) of small dimensions (DP of 5 and 7) is described for amylomaltase from the thermophilic bacterium Deinococcus geothermalis using as substrate the debranched products of amylomaize, instead of the usually used potato amylose or rice amylose
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Synthesis of cycloamyloses (CAs) of small dimensions (DP of 5 and 7) is described for amylomaltase from the thermophilic bacterium Deinococcus geothermalis using as substrate the debranched products of amylomaize, instead of the usually used potato amylose or rice amylose
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additional information
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Substrates: acts in concert with EC 2.4.1.1
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Substrates: acts in concert with EC 2.4.1.1
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Substrates: strain ML308, D-glucose, D-mannose, methyl-alpha-D-glucoside, phenyl-alpha-D-glucoside, methyl-alpha-D-mannoside and cellobiose have no activity as acceptors
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Substrates: maltose is inable to serve as a donor substrate, serving only as an acceptor substrate
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Substrates: D-galactose, sugar alcohols such as sorbitol and xylitol and glycerol are not effective as acceptors
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Substrates: does not act on maltitol, maltotriitol, glucosylsucrose, isomaltose, panose, isopanose or isomaltosylmaltose, enzyme does not catalyze hydrolytic action on maltotetraitol, maltopentaitol or maltosylsucrose, sorbitol and maltitol are not produced
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additional information
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Substrates: maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
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additional information
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Substrates: maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
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additional information
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Substrates: does not act on maltitol, maltotriitol, glucosylsucrose, isomaltose, panose, isopanose or isomaltosylmaltose, enzyme does not catalyze hydrolytic action on maltotetraitol, maltopentaitol or maltosylsucrose, sorbitol and maltitol are not produced
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additional information
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Substrates: does not act on maltitol, maltotriitol, glucosylsucrose, isomaltose, panose, isopanose or isomaltosylmaltose, enzyme does not catalyze hydrolytic action on maltotetraitol, maltopentaitol or maltosylsucrose, sorbitol and maltitol are not produced
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additional information
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Substrates: transglycosylation activity assay using starch as donor substrate, and glucose, maltose, maltotriose, maltotetraose, maltohexaose, and maltoheptaose as acceptor substrates, starch degradation is determined by the iodine solution method. D-glucose ist the preferred acceptor substrate, higher activity also with maltose and maltohexaose, lower activity with maltotriose and maltotetraose. The activity of enzyme Hw-A is much higher than that of commercial amylase from Bacillus licheniformis
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
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additional information
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Substrates: maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview
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additional information
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Substrates: major pathway for starch degradation in chloroplasts
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additional information
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Substrates: cannot use maltose or cyclohexaamylose as a substrate
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additional information
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Substrates: the enzyme produces oligosaccharides with degree of polymerization (DP) of DP22 to over DP60 from potato amylose
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additional information
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Substrates: the enzyme produces oligosaccharides with degree of polymerization (DP) of DP22 to over DP60 from potato amylose
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additional information
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Substrates: does not act on 6-O-alpha-maltosyl cyclomaltoheptaose
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additional information
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Substrates: 2 different enzyme activities, oligo-1,4-1,4-glucan-4-glycosyltransferase EC 2.4.1.25 and amylo-1,6-glucosidase EC 3.2.1.33 reside on the same polypeptide chain
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additional information
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Substrates: 2 different enzyme activities, oligo-1,4-1,4-glucan-4-glycosyltransferase EC 2.4.1.25 and amylo-1,6-glucosidase EC 3.2.1.33 reside on the same polypeptide chain
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additional information
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Substrates: glucose is the major product of the D-enzyme reaction
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additional information
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Substrates: maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview
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additional information
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Substrates: maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview
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additional information
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Substrates: maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview
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additional information
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Substrates: maltose, maltotriose, maltotetraose, and beta-cyclodextrin substrate binding enzyme structures, analysis and docking, overview
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additional information
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Substrates: acting on gelatinized food-grade potato starch, PyAMase produced a thermoreversible starch product with gelatin-like properties
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Kinetic values indicate the maximum efficiency (kcat/Km) for maltotriose, with decreasing values for the other substrates as their length increase
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Kinetic values indicate the maximum efficiency (kcat/Km) for maltotriose, with decreasing values for the other substrates as their length increase
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additional information
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Pyrobaculum aerophilum CIP 104966
Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Kinetic values indicate the maximum efficiency (kcat/Km) for maltotriose, with decreasing values for the other substrates as their length increase
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Kinetic values indicate the maximum efficiency (kcat/Km) for maltotriose, with decreasing values for the other substrates as their length increase
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Kinetic values indicate the maximum efficiency (kcat/Km) for maltotriose, with decreasing values for the other substrates as their length increase
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Kinetic values indicate the maximum efficiency (kcat/Km) for maltotriose, with decreasing values for the other substrates as their length increase
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Kinetic values indicate the maximum efficiency (kcat/Km) for maltotriose, with decreasing values for the other substrates as their length increase
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
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additional information
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Pyrobaculum calidifontis DSM 21063
Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
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additional information
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Substrates: the enzyme is involved in glycogen metabolism by selective cleavage of the outer side chain
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additional information
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Substrates: the enzyme exhibits hydrolyzing activity toward alpha-1,6-glycosidic linkages of amylopectin, glycogen, pullulan, and other branched substrates, glycogen is the preferred substrate, TreX shows high specificity for hydrolysis of maltohexaosyl alpha-1,6-beta-cyclodextrin, and high activity in 4-alpha-sulfoxide-glucantransferase activity transferring alpha-1,4-glucan oligosaccharides from one chain to another. The enzyme tetramer shows a 4fold higher catalytic activity than the dimer. The enzyme catalyzes intramolecular transglycosylation of maltooligosacchrides, i.e. disproportionation to produce linear alpha-1,4-glucans, as well as intramolecular transglycosylation of glycogen
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additional information
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Substrates: synthesis of di-O-alpha-maltosyl-beta-cyclodextrin from 6-O-alpha-maltosyl-beta-cyclodextrin via a transglycosylation reaction, TreX transfers the maltosyl residue of a G2-beta-cyclodextrin to another molecule of G2-beta-cyclodextrin by forming an alpha-1,6-glucosidic linkage. TreX shows specificity for a branched glucosyl chain bigger than DP2 and no activity toward glucosyl-beta-cyclodextrin, transglycosylation reaction mechanism, overview
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additional information
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Substrates: TreX from Sulfolobus solfataricus shows dual activities for alpha-1,4-transferase, EC 2.4.1.25 and alpha-1,6-glucosidase, EC 3.2.1.68, bifunctional mechanism, substrate maltotriose, overview. TreX exhibits two different active-site configurations depending on its oligomeric state
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additional information
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Substrates: TreX from Sulfolobus solfataricus shows dual activities for alpha-1,4-transferase, EC 2.4.1.25 and alpha-1,6-glucosidase, EC 3.2.1.68, bifunctional mechanism, substrate maltotriose, overview. TreX exhibits two different active-site configurations depending on its oligomeric state
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additional information
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Substrates: the enzyme is involved in glycogen metabolism by selective cleavage of the outer side chain
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additional information
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Substrates: the enzyme exhibits hydrolyzing activity toward alpha-1,6-glycosidic linkages of amylopectin, glycogen, pullulan, and other branched substrates, glycogen is the preferred substrate, TreX shows high specificity for hydrolysis of maltohexaosyl alpha-1,6-beta-cyclodextrin, and high activity in 4-alpha-sulfoxide-glucantransferase activity transferring alpha-1,4-glucan oligosaccharides from one chain to another. The enzyme tetramer shows a 4fold higher catalytic activity than the dimer. The enzyme catalyzes intramolecular transglycosylation of maltooligosacchrides, i.e. disproportionation to produce linear alpha-1,4-glucans, as well as intramolecular transglycosylation of glycogen
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additional information
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Substrates: synthesis of di-O-alpha-maltosyl-beta-cyclodextrin from 6-O-alpha-maltosyl-beta-cyclodextrin via a transglycosylation reaction, TreX transfers the maltosyl residue of a G2-beta-cyclodextrin to another molecule of G2-beta-cyclodextrin by forming an alpha-1,6-glucosidic linkage. TreX shows specificity for a branched glucosyl chain bigger than DP2 and no activity toward glucosyl-beta-cyclodextrin, transglycosylation reaction mechanism, overview
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additional information
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Substrates: appears to be exclusively oligo-1,4-1,4-glucantransferase-amylo 1,6-glucosidase and does not have isoamylase
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Substrates: does not act on 6-O-alpha-maltosyl cyclomaltoheptaose
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additional information
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Substrates: 2 different enzyme activities, oligo-1,4-1,4-glucan-4-glycosyltransferase EC 2.4.1.25 and amylo-1,6-glucosidase EC 3.2.1.33 reside on the same polypeptide chain
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additional information
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Substrates: glucose is the major product of the D-enzyme reaction
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additional information
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Substrates: maltose is not a donor substrate, only weak acceptor activity
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Substrates: glucose is the major product of the D-enzyme reaction
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Substrates: glucose is the major product of the D-enzyme reaction
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Substrates: D-glucosamine, N-acetyl-D-glucosamine and isomaltose have no activity as acceptors
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Substrates: maltose is not a product
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Substrates: maltose is not a product
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Substrates: maltose is not a product
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Substrates: maltose is not a product
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Substrates: maltose is no substrate
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additional information
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Substrates: maltose is no substrate
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Substrates: the enzyme produces oligosaccharides with degree of polymerization (DP) of DP17 to over DP100 from synthetic amylose
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Substrates: glucose is the major product of the D-enzyme reaction
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
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additional information
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Substrates: the enzyme produces oligosaccharides with degree of polymerization (DP) of DP22-DP50 from pea starch
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additional information
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Streptococcus agalactiae YZ1605
Substrates: the enzyme produces oligosaccharides with degree of polymerization (DP) of DP22-DP50 from pea starch
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Substrates: acts in concert with EC 2.4.1.1
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additional information
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Substrates: acts in concert with EC 2.4.1.1
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additional information
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Substrates: D-enzyme, maltohexaose is no initial substrate
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additional information
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-
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Substrates: 2 glycosyltransferases, amylomaltase and D-enzyme
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additional information
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-
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Substrates: Glcalpha1-4Glcalpha1-4Glcalpha1-4Glcalpha1-4Glcalpha1-4(Glcalpha1-4Glcalpha1-4 Glcalpha1-4Glcalpha1-6)Glcalpha1-4Glcalpha1-4Glc-maltose, Glcalpha1-4Glcalpha1-4 Glcalpha1-4Glcalpha1-4(Glcalpha1-4Glcalpha1-4Glcalpha1-4Glcalpha1-6)Glcalpha1-4 Glcalpha1-4Glcalpha1-4Glc-maltose or Glcalpha1-4Glcalpha1-4Glcalpha1-4(Glcalpha1-4 Glcalpha1-4Glcalpha1-4Glcalpha1-6)Glcalpha1-4Glcalpha1-4Glcalpha1-4Glcalpha1-4Glc-maltose are suitable fluorogenic substrates for assaying debranching enzyme
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additional information
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Substrates: the enzyme liberates maltose oligomers from branched dextrins in presence or absence of acceptor maltohexaose, 6_4-O-alpha-glucosyl-pyridylamino-maltooctaose is liberated from 64-O-alpha-maltopentaosyl-pyridylamino-maltooctaose, 64-O-alpha-maltotetraosyl-pyridylamino-maltooctaose and 64-O-alpha-maltotriosyl-pyridylamino-maltooctaose, whereas 64-O-alpha-maltosyl-pyridylamino-maltooctaose is resistant to the enzyme, donor substrate specificity of GDE, GDE 4-alpha-glucanotransferase removes a maltotriosyl residue from the maltotetraosyl branch in a way that the alpha-1,6-linked glucosyl residue is retained, overview
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additional information
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Substrates: analysis of the substrate specificities of 4-alpha-glucanotransferase and amylo-alpha-1,6-glucosidase (EC 3.2.1.33) using fluorogenic biantennary dextrins such as G-GG-G-(G-G-G-G<->)G-G-GPA (F4/4/2, where GPA = 1-deoxy-1-[(2-pyridyl)amino]-D-glucitol), G-(G-G-G-G<->)G-G-GPA (F1/4/2), and G-G-G-G-G-G-G-(G<->)G-G-GPA (F7/1/2). Contrary to the prevailing hypothesis, the main branch of F4/4/2 is an important donor substrate component of 4-alpha-glucanotransferase and does not serve as an acceptor substrate. But when G-G-G-G-G-GPA is added to the mixture, it successfully accepts a maltotriosyl (G3-) residue from F4/4/2. The debranching activity of GDE towards phosphorylase-limit glycogen substantially increases when methyl alpha-maltooligosides with lengths equal to or greater than that of methyl alpha-maltopentaoside (G5-OCH3) are added to the enzyme reaction mixture. GP-limit dextrin is a bifunctional substrate possessing both donor and acceptor moieties for GDE 4-alpha-glucanotransferase. Maltohexaose is both acceptor and activator of 4-alpha-glucanotransferase. Synthesis of fluorogenic biantennary dextrins F3/1/2, F4/1/2, F5/1/2, F4/1/3, F1/4/2, F4/4/2, and F4/4/3. Substrate specificity of GDE 4-alpha-glucanotransferase, overview
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additional information
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Substrates: glucose is the major product of the D-enzyme reaction
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additional information
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Substrates: the enzyme displays transglycosylating activity on various maltooligosaccharides, e.g. corn starches consisting of different proportions of amylopectin and amylose, of which the smallest donor and acceptor molecules are determined to be maltose and glucose, respectively, overview. Activity of alphaGTase decreases amylopectin and increases cycloamylose contents in the polymers, product determination by MALDI-TOF-MS analysis, product molecular weight and branch-chain distribution after isoamylolysis of different starches, overview
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additional information
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Substrates: the enzyme produces oligosaccharides with degree of polymerization (DP) of DP24-DP284 from sucrose and of DP12-DP36 from corn starch
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additional information
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Therminus sp.
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Substrates: alpha- and beta-arbutin-alpha-D-glycosides are formed through transglycosylation reactions catalyzed by a recombinant amylomaltase, using tapioca starch and alpha- and beta-arbutin as donor and acceptor molecules, respectively. The glycoside products are isolated and analyzed by HPLC, and two major products are identified by mass spectrometry and nuclear magnetic resonance spectroscopy, namely, alpha-arbutin-alpha-D-glucopyranoside (alpha-Ab-alpha-G1) and alpha-arbutin-alpha-D-maltopyranoside (alpha-Ab-alpha-G2). Both alpha-Ab-alpha-G1 and alpha-Ab-alpha-G2 are more water soluble than alpha-arbutin
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additional information
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Substrates: enzyme catalyzes not only intermolecular transglycosylation to produce linear alpha-1,4-glucan, but also intramolecular transglycosylation to produce cyclic alpha-1,4-glucan
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
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additional information
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-
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Substrates: 2 different 4-alpha-glucanotransferases, MTAse and Gtase
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additional information
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-
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Substrates: unable to use maltotriose as donor sugar or glucose as acceptor sugar
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additional information
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-
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Substrates: Gtase, glucose does not function as acceptor sugar, nor does it appear as reaction product
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additional information
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-
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Substrates: maltose and maltotriose are not disproportionated, glucose does not function as an acceptor sugar in transfer reactions, glucose also never appears as a reaction product
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additional information
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-
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Substrates: alpha-D-glucose, beta-D-fructose, D-ribose, D-arabinose, D-xylose, isomaltose, D-trehalose, D-cellobiose, lactose, sucrose, raffinose and N-acetyl-D-glucosamine cannot participate as acceptor sugars in glucanosyl transfer from amylose
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additional information
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Substrates: polysaccharides, such as soluble starch, amylose and amylopectin, and maltooligosaccharides longer than maltose can be effective maltosyl group donors for the enzyme. All maltooligosaccharides are able to act as acceptor molecules in 4-alpha-glucanotransferase-mediated transfer of glucan segments from amylose
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additional information
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Substrates: modification of granular corn starch with 4-alpha-glucanotransferase from Thermotoga maritima without induction of gelatinization, analysis of the morphology of the modified starches with light and scanning electron microscopy, the granule integrity is mostly maintained after enzyme treatment, although some granules are partially fragmented, amylose and amylopectin levels can be altered, solubility and paste clarity of themodified starches are much higher than those of raw starch, and it shows thermoreversibility between 4 and 75°C, X-ray diffraction and relative crystallinity, overview
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additional information
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Substrates: modification of granular corn starch with 4-alpha-glucanotransferase from Thermotoga maritima without induction of gelatinization, analysis of the morphology of the modified starches with light and scanning electron microscopy, the granule integrity is mostly maintained after enzyme treatment, although some granules are partially fragmented, amylose and amylopectin levels can be altered, solubility and paste clarity of themodified starches are much higher than those of raw starch, and it shows thermoreversibility between 4 and 75°C, X-ray diffraction and relative crystallinity, overview
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additional information
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Substrates: 4-nitrophenyl-alpha-D-glucopyranoside, 4-nitrophenyl-alpha-D-maltotrioside, 4-methylumbelliferyl-alpha-D-glucopyranoside, and 5-bromo-4-chloro-3-indolyl-alpha-D-glucopyranoside are acceptors for GTase
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additional information
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Substrates: the enzyme catalyses the transfer of maltosyl units from alpha-1,4-linked glucans or malto-oligosaccharides to other alpha-1,4-linked glucans, maltooligosaccharides or glucose
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additional information
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Substrates: the enzyme catalyses the transfer of maltosyl units from alpha-1,4-linked glucans or malto-oligosaccharides to other alpha-1,4-linked glucans, maltooligosaccharides or glucose
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additional information
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Substrates: GTase displays a broad transfer specificity
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Substrates: GTase displays a broad transfer specificity
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additional information
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Substrates: the enzyme is highly specialised on the transfer of maltosyl residues from aalpha-1,4-linked glucans or malto-oligosaccharides to other alpha-1,4-linked glucans, malto-oligosaccharides, or glucose
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additional information
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Substrates: the enzyme is highly specialised on the transfer of maltosyl residues from aalpha-1,4-linked glucans or malto-oligosaccharides to other alpha-1,4-linked glucans, malto-oligosaccharides, or glucose
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additional information
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Substrates: 4-nitrophenyl-alpha-D-glucopyranoside, 4-nitrophenyl-alpha-D-maltotrioside, 4-methylumbelliferyl-alpha-D-glucopyranoside, and 5-bromo-4-chloro-3-indolyl-alpha-D-glucopyranoside are acceptors for GTase
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additional information
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Substrates: the enzyme catalyses the transfer of maltosyl units from alpha-1,4-linked glucans or malto-oligosaccharides to other alpha-1,4-linked glucans, maltooligosaccharides or glucose
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additional information
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Substrates: the enzyme catalyses the transfer of maltosyl units from alpha-1,4-linked glucans or malto-oligosaccharides to other alpha-1,4-linked glucans, maltooligosaccharides or glucose
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additional information
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Substrates: GTase displays a broad transfer specificity
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additional information
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Substrates: GTase displays a broad transfer specificity
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additional information
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Substrates: the enzyme is highly specialised on the transfer of maltosyl residues from aalpha-1,4-linked glucans or malto-oligosaccharides to other alpha-1,4-linked glucans, malto-oligosaccharides, or glucose
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additional information
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-
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Substrates: TAalphaGT catalyzes the transfer of glucose units from one 1,4-alpha-glucan to another and requires at least maltose units for the disproportionation reaction
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additional information
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B7A9X4
Substrates: amylomaltase from Thermus aquaticus catalyzes three types of transglycosylation reaction, as well as a weak hydrolytic reaction of alpha-1,4 glucan
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additional information
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-
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Substrates: amylomaltase from Thermus aquaticus catalyzes three types of transglycosylation reaction, as well as a weak hydrolytic reaction of alpha-1,4 glucan
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additional information
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B7A9X4
Substrates: the enzyme contains two substrate binding sites involving residues Y54 or Y101, structure and localization, overview. The binding of glucan substrate to the second glucan binding site through an interaction with the aromatic side chains of Y54 and Y101 is a trigger for the enzyme to take a completely active conformation for all four types of activity, but prevents the cyclization reaction to occur since the flexibility of the glucan is restricted by such binding. Synthesis of cycloamylose, overview
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additional information
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Substrates: the enzyme contains two substrate binding sites involving residues Y54 or Y101, structure and localization, overview. The binding of glucan substrate to the second glucan binding site through an interaction with the aromatic side chains of Y54 and Y101 is a trigger for the enzyme to take a completely active conformation for all four types of activity, but prevents the cyclization reaction to occur since the flexibility of the glucan is restricted by such binding. Synthesis of cycloamylose, overview
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additional information
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-
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Substrates: the enzyme modifies corn starch with different amylose contents leading to a broader chain-length distribution of the of isoamylolytically debranched products, formation of a variety of cycloamyloses with different sizes, MALDI-TOF-MS analysis of cycloamyloses, overview
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additional information
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-
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Substrates: the enzyme catalyzes an inter-molecular transglycosylation, by transfer of alpha glucan moiety from one alpha-1,4-glucan molecule to another or to glucose, forming two linear products of different sizes
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additional information
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Substrates: modification of rice starch by the enzyme
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Products have a degree of polymerization between 19 and 35. Cyclization is favored by raising the temperature to 70°C and lowering the pH to 5. Synthesis of cycloamyloses (CAs) of small dimensions (DP of 5 and 7) is also described for amylomaltase from the thermophilic bacterium Thermus aquaticus using as substrate the debranched products of amylomaize, instead of the usually used potato amylose or rice amylose
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additional information
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Substrates: the enzyme produces oligosaccharides with degree of polymerization (DP) of DP22 to over DP60 from synthetic amylose
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additional information
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Thermus aquaticus ATCC 33923
Substrates: the enzyme produces oligosaccharides with degree of polymerization (DP) of DP22 to over DP60 from synthetic amylose
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additional information
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-
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Substrates: TAalphaGT catalyzes the transfer of glucose units from one 1,4-alpha-glucan to another and requires at least maltose units for the disproportionation reaction
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additional information
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-
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Substrates: the enzyme reacts with small oligosaccharides, especially maltotriose, to form various maltooligosaccharides by using its disproportionating activity
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Enzyme specific activity of amylomaltase from Thermus brockianus decreases from maltotriose to maltoheptaose
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Maltotriose is the most effective substrate for the Thermus filiformis enzyme, products have a degree of polymerization between 22 and 29
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additional information
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Substrates: the enzyme produces oligosaccharides with degree of polymerization (DP) of DP22-DP60 from pea starch
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additional information
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-
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Substrates: rice cake production using a thermostable 4-alpha-glucanotransferase from Thermus scotoductus, starch molecular fine structure, texture, and retrogradation, the number of shorter side chains increases, whereas the number of longer side chains decreases through the disproportionation reaction of TSalphaGTase, amylose and malto-oligosaccharide contents are altered, molecular weight of rice starch, overview
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additional information
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-
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Substrates: the enzyme acts on rice starch and modulates the starch concerning concentration, flow behavior, gel strength, and melting and gelling kinetics. As the level of enzyme decreases and the starch concentration increases, gelation time decreases and the final gel strength increased significantly. Regardless of treatment variables, all the modified starch gels melt at similar temperature, dynamic rheological behavior of enzyme-treated rice starch paste, overview
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additional information
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Substrates: the enzyme acts on rice starch and amylopectin, the alpha-1,4 glucosidic linkage of the segment between amylopectin clusters is hydrolyzed with a rearrangement in the side-chain length distribution, the highly branched amylopectin cluster, HBAPC, and highly branched amylose, HBA contain significant numbers of branched maltooligosaccharide side chains, HBAPC and HBA show higher water solubility and stability against retrogradation than amylopectin clusters or branched amylose, overview
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additional information
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-
Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Synthesis of cycloamyloses (CAs) of small dimensions (DP of 5 and 7) is described for amylomaltase from the thermophilic bacterium Thermus scotoductus using as substrate the debranched products of amylomaize, instead of the usually used potato amylose or rice amylose
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additional information
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Substrates: scale-up preparation and purification of synthesized maltotriosyl-erythritol (EG3) derivatives, overview. The main transfer product of 1-O- and 4-O-forms may be a mixture of equal amounts, EG3 ought to be connected to erythritol through three alpha-configurations as a result of the particular transglycosylation activity of alpha-AMase. Generally, it seems that the type of alpha- or beta-glycosidic linkage that formed between the acceptor and donor is based on the enzyme that is used in the transglycosylation reaction
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additional information
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Substrates: glucose can only be used as acceptor of maltosyl units
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additional information
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Substrates: Thermus thermophilus AMase is among the most efficient 4-alpha-glucanotransferases in the alpha-amylase superfamily
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additional information
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Substrates: amylomaltases are capable of the synthesis of large cyclic glucans and the disproportionation of oligosaccharides
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additional information
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Substrates: substrates are maltooligomers, trimer to heptamer, substrate binding mechanism and structure, modeling. The active site contains at least seven substrate binding sites, subsites -2 and +3 favoring substrate binding and subsites -3 and +2 do not, substrate specificity, overview
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additional information
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Substrates: glucose transfer/production using maltose and glycogen. Wild-type DPE2 can bind to starch and glycogen has very little, if any, ability to dissociate DPE2 from the starch pellet
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additional information
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Substrates: preparation of gels from starches of various botanical origin, e.g. potato, high amylose potato, maize, waxy maize, wheat and pea starches, by modification through the enzyme from Thermus thermophilus, thermodynamics and product properties, overview
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Maltotetraose and maltopentaose are the most effective substrates for the Thermus thermophilus enzyme
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Maltotetraose and maltopentaose are the most effective substrates for the Thermus thermophilus enzyme
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additional information
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Substrates: in the crumb of fresh white wheat bread, starch is fully gelatinized. Its molecular and three-dimensional structure are major factors limiting the rate of its digestion. In situ modification of starch during bread making with starch-modifying enzymes (maltogenic amylase and amylomaltase) and analysis of the impact thereof on bread characteristics, starch retrogradation and digestibility, overview. Maltogenic amylase treatment increases the relative content of short amylopectin chains. This results in lower starch retrogradation and crumb firmness upon storage, and reduces extent (up to 18%) of in vitro starch digestion for fresh and stored breads. Amylomaltase only modestly shortens amylose chains and has no measurable impact on amylopectin structure. Modification with this enzyme leads to slower bread crumb firming but does not influence starch digestibility, detailed overview. In vitro analysis of starch digestion in freeze-dried bread crumb
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Maltotetraose and maltopentaose are the most effective substrates for the Thermus thermophilus enzyme
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Maltotetraose and maltopentaose are the most effective substrates for the Thermus thermophilus enzyme
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additional information
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Substrates: amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Maltotetraose and maltopentaose are the most effective substrates for the Thermus thermophilus enzyme
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additional information
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Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Substrates: Thermus thermophilus AMase is among the most efficient 4-alpha-glucanotransferases in the alpha-amylase superfamily
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additional information
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Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Substrates: substrates are maltooligomers, trimer to heptamer, substrate binding mechanism and structure, modeling. The active site contains at least seven substrate binding sites, subsites -2 and +3 favoring substrate binding and subsites -3 and +2 do not, substrate specificity, overview
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additional information
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Substrates: glucose is the major product of the D-enzyme reaction
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additional information
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Substrates: cannot use maltose or cyclohexaamylose as a substrate
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
maltodextrin + maltose
maltooligosaccharides + alpha-D-glucose
Substrates: -
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1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
Substrates: it is proposed that a soluble heteroglycan is the in vivo substrate for DPE2. An alternative route to metabolize the glucan residues in soluble heteroglycane exists in Arabidopsis thaliana
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1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
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Substrates: it is proposed that a soluble heteroglycan is the in vivo substrate for DPE2. An alternative route to metabolize the glucan residues in soluble heteroglycan exists in Escherichia coli
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maltodextrin + maltose
maltooligosaccharides
-
Substrates: catabolic processing of glycogen and maltodextrins
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maltodextrin + maltose
maltooligosaccharides
Substrates: -
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maltodextrin + maltose
maltooligosaccharides
-
Substrates: catabolic processing of glycogen and maltodextrins
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maltodextrin + maltose
maltooligosaccharides
-
Substrates: catabolic processing of glycogen and maltodextrins
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maltopentaose + maltopentaose
maltooligosaccharides
-
Substrates: metabolism of starch in the bacterium
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maltopentaose + maltopentaose
maltooligosaccharides
-
Substrates: metabolism of starch in the bacterium
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maltopentaose + maltopentaose
maltooligosaccharides
-
Substrates: metabolism of starch in the bacterium
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maltopentaose + maltopentaose
maltooligosaccharides
-
Substrates: metabolism of starch in the bacterium
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maltopentaose + maltopentaose
maltooligosaccharides
-
Substrates: metabolism of starch in the bacterium
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maltopentaose + maltopentaose
maltooligosaccharides
-
Substrates: metabolism of starch in the bacterium
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maltopentaose + maltopentaose
maltooligosaccharides
Stutzerimonas stutzeri NRRL B3389
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Substrates: metabolism of starch in the bacterium
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maltopentaose + maltopentaose
maltooligosaccharides
-
Substrates: metabolism of starch in the bacterium
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maltopentaose + maltopentaose
maltooligosaccharides
-
Substrates: metabolism of starch in the bacterium
Products: -
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additional information
?
-
-
Substrates: amylomaltase is involved in the conversion of maltose to sucrose in the cytosol
Products: -
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additional information
?
-
Substrates: 4-alpha-glucanotransferase is essential for maltose metabolism in photosynthetic leaves
Products: -
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additional information
?
-
-
Substrates: the enzyme is involved in glycogen metabolism by selective cleavage of the outer side chain
Products: -
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additional information
?
-
-
Substrates: the enzyme is involved in glycogen metabolism by selective cleavage of the outer side chain
Products: -
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additional information
?
-
B7A9X4
Substrates: amylomaltase from Thermus aquaticus catalyzes three types of transglycosylation reaction, as well as a weak hydrolytic reaction of alpha-1,4 glucan
Products: -
Products: -
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additional information
?
-
-
Substrates: amylomaltase from Thermus aquaticus catalyzes three types of transglycosylation reaction, as well as a weak hydrolytic reaction of alpha-1,4 glucan
Products: -
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additional information
?
-
Substrates: Thermus thermophilus AMase is among the most efficient 4-alpha-glucanotransferases in the alpha-amylase superfamily
Products: -
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additional information
?
-
Substrates: amylomaltases are capable of the synthesis of large cyclic glucans and the disproportionation of oligosaccharides
Products: -
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additional information
?
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Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Substrates: Thermus thermophilus AMase is among the most efficient 4-alpha-glucanotransferases in the alpha-amylase superfamily
Products: -
Products: -
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
no metal ions are required for activity or stability of the enzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
aplanin
-
Bay e 4609, pseudooligosaccharide resembling amylose with a hydroxymethylconduritol unit and a 4-amino-4-deoxy-D-chinorose residue linked to a varying number of alpha-D-glucose units from 7-30
NaCl
-
80% inhibition of starch transglycosylation activity at 0.5-4 M NaCl
acarbose
a strong mixed inhibitor with almost equal competitive and uncompetitive binding constants, acarbose is both bound in the active site and at another site
additional information
toxic BinA component of the activated binary toxin does not inhibit alpha-glucosidase activity of the enzyme, while BinB reduces the activity by nearly 50%
-
additional information
-
toxic BinA component of the activated binary toxin does not inhibit alpha-glucosidase activity of the enzyme, while BinB reduces the activity by nearly 50%
-
additional information
addition of Mg2+, K+, or EDTA does not significantly affect the activity
-
additional information
neither CaCl2, MgCl2, BaCl2, NiCl2 or CoCl2 (all at 1 mM) nor 50-200 mM NaCl or 50-200 mM EDTA have a significant influence on transferase activity
-
additional information
-
neither CaCl2, MgCl2, BaCl2, NiCl2 or CoCl2 (all at 1 mM) nor 50-200 mM NaCl or 50-200 mM EDTA have a significant influence on transferase activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cyclodextrin
-
the extent of 4-alpha-glucanotransferase activation increases with cyclodextrin concentration before reaching a constant value
-
maltoheptaose
-
stimulating effect of maltooligosaccharides on the conversion of amylose, 15 mM, relative activity 124%
maltohexaose
-
stimulating effect of maltooligosaccharides on the conversion of amylose, 15 mM, relative activity 144%
maltopentaose
-
stimulating effect of maltooligosaccharides on the conversion of amylose, 15 mM, relative activity 210%
maltose
-
stimulating effect of maltooligosaccharides on the conversion of amylose, relative activity 259%
maltotetraose
-
stimulating effect of maltooligosaccharides on the conversion of amylose, 15 mM, relative activity 246%
maltotriose
-
stimulating effect of maltooligosaccharides on the conversion of amylose, 15 mM, relative activity 210%
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
4-alpha-glucanotransferase deficiency
Biochemical characterization of the chlamydomonas reinhardtii alpha-1,4 glucanotransferase supports a direct function in amylopectin biosynthesis
Anemia, Hypochromic
Blocking the metabolism of starch breakdown products in Arabidopsis leaves triggers chloroplast degradation.
Carcinoma
Co-expression of alpha(1,3)galactosyltransferase and Bacillus thuringiensis PIPLC enhances hyperacute rejection of tumor cells.
Glycogen Storage Disease
A mutation analysis of the AGL gene in Korean patients with glycogen storage disease type III.
Glycogen Storage Disease
Clinical and genetic variability of glycogen storage disease type IIIa: seven novel AGL gene mutations in the Mediterranean area.
Glycogen Storage Disease
Molecular characterisation of GSD III subjects and identification of six novel mutations in AGL.
Glycogen Storage Disease Type III
A mutation analysis of the AGL gene in Korean patients with glycogen storage disease type III.
Glycogen Storage Disease Type III
Clinical and genetic variability of glycogen storage disease type IIIa: seven novel AGL gene mutations in the Mediterranean area.
Glycogen Storage Disease Type III
Molecular characterisation of GSD III subjects and identification of six novel mutations in AGL.
Leprosy
Mycobacterium leprae specific genomic target in the promoter region of probable 4-alpha-glucanotransferase (ML1545) gene with potential sensitivity for polymerase chain reaction based diagnosis of leprosy.
Lyme Disease
The unique glycoside hydrolase family 77 amylomaltase from Borrelia burgdorferi with only catalytic triad conserved.
Neoplasms
Co-expression of alpha(1,3)galactosyltransferase and Bacillus thuringiensis PIPLC enhances hyperacute rejection of tumor cells.
Tuberculosis
Mycobacterium tuberculosis maltosyltransferase GlgE, a genetically validated antituberculosis target, is negatively regulated by Ser/Thr phosphorylation.
Tuberculosis
Self-poisoning of Mycobacterium tuberculosis by targeting GlgE in an alpha-glucan pathway.
Tuberculosis
Synthesis of a C-phosphonate mimic of maltose-1-phosphate and inhibition studies on Mycobacterium tuberculosis GlgE.
Virus Diseases
RNA interference-based antiviral immune response against the salivary gland hypertrophy virus in Glossina pallidipes.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0718
starch
pH 6.0, 30°C, starch transglycosylation, recombinant mutant G417F
0.0741
starch
pH 6.0, 30°C, starch transglycosylation, recombinant mutant P228Y
0.0822
starch
pH 6.0, 30°C, starch transglycosylation, recombinant wild-type enzyme
0.14
starch
pH 6.0, 30°C, starch transglycosylation, recombinant mutant Y23A
0.186
starch
pH 6.0, 30°C, starch transglycosylation, recombinant mutant E231Y
12.27
starch
pH 6.0, 30°C, disproportionation activity, recombinant mutant Y23A
15.4
starch
pH 6.0, 30°C, disproportionation activity, recombinant mutant E231Y
18.1
starch
pH 6.0, 30°C, disproportionation activity, recombinant wild-type enzyme
19.7
starch
pH 6.0, 30°C, disproportionation activity, recombinant mutant P228Y
22.9
starch
pH 6.0, 30°C, disproportionation activity, recombinant mutant G417F
additional information
additional information
kinetics of wild-type and mutant enzymes at pH 6.5 and 70°C, overview
-
additional information
additional information
initial rate kintics
-
additional information
additional information
-
at 25 mM alpha-cyclodextrin, the reaction rate decreases with increasing dodecyl-beta-maltoside concentration, and when the alpha-cyclodextrin concentration is varied at fixed dodecyl-beta-maltoside concentration, an S shaped curve is obtained
-
additional information
additional information
Michaelis-Menten kinetic analysis
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000755
starch
pH 6.0, 30°C, cyclization activity, recombinant mutant G417F
0.00157
starch
pH 6.0, 30°C, cyclization activity, recombinant mutant Y23A
0.00228
starch
pH 6.0, 30°C, cyclization activity, recombinant mutant P228Y
0.00277
starch
pH 6.0, 30°C, cyclization activity, recombinant wild-type enzyme
0.00279
starch
pH 6.0, 30°C, cyclization activity, recombinant mutant E231Y
0.00545
starch
pH 6.0, 30°C, starch transglycosylation, recombinant mutant G417F
0.00625
starch
pH 6.0, 30°C, starch transglycosylation, recombinant mutant Y23A
0.0073
starch
pH 6.0, 30°C, starch transglycosylation, recombinant wild-type enzyme
0.0073
starch
pH 6.0, 30°C, starch transglycosylation, recombinant mutant P228Y
0.017
starch
pH 6.0, 30°C, starch transglycosylation, recombinant mutant E231Y
43.83
starch
pH 6.0, 30°C, disproportionation activity, recombinant mutant P228Y
103
starch
pH 6.0, 30°C, disproportionation activity, recombinant wild-type enzyme
110.8
starch
pH 6.0, 30°C, disproportionation activity, recombinant mutant Y23A
111.3
starch
pH 6.0, 30°C, disproportionation activity, recombinant mutant E231Y
139.5
starch
pH 6.0, 30°C, disproportionation activity, recombinant mutant G417F
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0448
starch
pH 6.0, 30°C, starch transglycosylation, recombinant mutant Y23A
0.0773
starch
pH 6.0, 30°C, starch transglycosylation, recombinant mutant G417F
0.0957
starch
pH 6.0, 30°C, starch transglycosylation, recombinant wild-type enzyme
0.0957
starch
pH 6.0, 30°C, starch transglycosylation, recombinant mutant E231Y
0.099
starch
pH 6.0, 30°C, starch transglycosylation, recombinant mutant P228Y
2.23
starch
pH 6.0, 30°C, disproportionation activity, recombinant mutant P228Y
5.7
starch
pH 6.0, 30°C, disproportionation activity, recombinant wild-type enzyme
6.09
starch
pH 6.0, 30°C, disproportionation activity, recombinant mutant G417F
7.23
starch
pH 6.0, 30°C, disproportionation activity, recombinant mutant E231Y
9.03
starch
pH 6.0, 30°C, disproportionation activity, recombinant mutant Y23A
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0556
beta-cyclodextrin
-
pH 5.5, 75°C, recombinant His-tagged enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.9
44.2
47.5
5.84
690
additional information
additional information
-
Glcalpha1-4Glcalpha1-4Glcalpha1-4Glcalpha1-4Glcalpha1-4(Glcalpha1-4Glcalpha1-4 Glcalpha1-4Glcalpha1-6)Glcalpha1-4Glcalpha1-4Glc-maltose, Glcalpha1-4Glcalpha1-4 Glcalpha1-4Glcalpha1-4(Glcalpha1-4Glcalpha1-4Glcalpha1-4Glcalpha1-6)Glcalpha1-4 Glcalpha1-4Glcalpha1-4Glc-maltose or Glcalpha1-4Glcalpha1-4Glcalpha1-4(Glcalpha1-4 Glcalpha1-4Glcalpha1-4Glcalpha1-6)Glcalpha1-4Glcalpha1-4Glcalpha1-4Glcalpha1-4Glc-maltose are suitable fluorogenic substrates for assaying debranching enzyme
additional information
B7A9X4
disproportionation and coupling activities of wild-type and Y54 mutated enzymes, overview
additional information
-
disproportionation and coupling activities of wild-type and Y54 mutated enzymes, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.2
5.5
5.5 - 6
6 - 7
6 - 8
6.5
6.7
6.9
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 7.5
pH dependence of wild-type and mutant enzymes, D293N and E340Q are active below pH 6.5 and pH 5.5, respectively, but precipitate during the necessary prolonged incubation times, wild-type Tt AMase precipitates below pH 5.5 under similar extended incubation times as well, overview
5 - 8
-
about 20% of maximal starch transglycosylation activity at pH 6.2-8.0, maximal activity at pH 5.2
5.2 - 7.5
more than 50% relative activity at pH values between 5.2 and 7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
35
37
40
45
60
70
70 - 75
75
80
85 - 90
90
95
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 70
-
about 20% of maximal starch transglycosylation activity at 30-50°C, 80% at 60°C, and maximal activity at 70°C, loss of activity at 80°C, inactive at 90°C
60 - 100
-
60°C: about 50% of maximal activity, 100°C: about 30% of maximal activity
65 - 95
more than 50% relative activity at temperatures between 65°C and 95°C
70 - 105
70°C: about 60% of maximal activity, 105°C: about 50% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.1
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strains CBS 513.88, NRRL3122, and N402, isozymes AgtA and AgtB encoded by genes agtA and agtB
-
-
brenda
Lyme disease spirochaete, strain BB0166, gene malQ
UniProt
brenda
alpha-1,4-glucanotransferase gene, GenBank accession no.
Uniprot
brenda
-
488997, 488998, 489001, 489002, 489003, 489009, 489014, 489016, 489018, 489019, 489021, 489023, 676621
-
-
brenda
isolated from the crystallization pond 'Imperatrice' (36% of salinity, 30°C, pH 7.2) of the Margherita di Savoia saltern, located on the south-eastern coast of Italy on June 2017
-
-
brenda
ATCC 33923, nucleotide sequence accession number, deposited in DDBJ/EMBL/GenBank
B7A9X4
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the enzyme is present in the amyloplast of developing endosperm
brenda
-
enzyme is more active in longissimus dorsi than in masseter. In both muscles the activity begins to fall at temperatures below 39°C and is almost zero when the temperature decreases to below 15°C. The activity of GDE may control the rate of glycogenolysis and glycolysis, but does not block rapid glycolysis and pH decrease when the temperature is high
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the enzyme contains a TIM barrel structure
brenda
-
the enzyme contains a TIM barrel structure
-
brenda
-
the enzyme contains a TIM barrel structure
-
brenda
-
the enzyme contains a TIM barrel structure
-
brenda
-
the enzyme contains a TIM barrel structure
-
brenda
-
the enzyme contains a TIM barrel structure
-
brenda
-
the enzyme contains a TIM barrel structure
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
evolution
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
evolution
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
evolution
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
evolution
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
evolution
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
evolution
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
evolution
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
evolution
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
evolution
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
evolution
the enzyme belongs to the glycoside hydrolase family 77, GH77. The N-terminal domains of G77 members may represent a distinct type of starch-binding domain and define a distinct CBM family, which is supported by studying docking of maltooligosaccharides to the N-terminal domain in amylomaltases, representing the four clusters of the phylogenetic tree, preliminary evolutionary distribution of all 100 GH77 amylomaltases into four groups, sequence comparisons, overview
evolution
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77, which contains specific 4-alpha-glucanotransferases identified only in plants and algae (known as disproportionating or D-enzymes) and in prokaryotes (amylomaltases). Most of the GH77 enzymes reported in CAZy are of bacterial origin, while only few are from Archaea, plants, and algae. The gene encoding the amylomaltase in halophilic archaeon Haloquadratum walsbyi is not part of any operon involved in the metabolism of maltooligosaccharides or glycogen, as it has been found in bacteria. The gene has specific insertions yet unknown in homologous genes in prokaryotes, and present only in amylomaltase genes identified in the genomes of other Haloquadratum walsbyi strains. Amylomaltases can be classified in at least four distinct groups, structural features, overview
evolution
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
evolution
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
evolution
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
evolution
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
evolution
the enzyme belongs to the glycoside hydrolase family 77, GH77. The N-terminal domains of G77 members may represent a distinct type of starch-binding domain and define a distinct CBM family, which is supported by studying docking of maltooligosaccharides to the N-terminal domain in amylomaltases, representing the four clusters of the phylogenetic tree, preliminary evolutionary distribution of all 100 GH77 amylomaltases into four groups, sequence comparisons, overview
evolution
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
evolution
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
evolution
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
evolution
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
evolution
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
evolution
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
evolution
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
evolution
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
evolution
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
evolution
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
evolution
the enzyme belongs to the glycoside hydrolase family 77, GH77. The N-terminal domains of G77 members may represent a distinct type of starch-binding domain and define a distinct CBM family, which is supported by studying docking of maltooligosaccharides to the N-terminal domain in amylomaltases, representing the four clusters of the phylogenetic tree, preliminary evolutionary distribution of all 100 GH77 amylomaltases into four groups, sequence comparisons, overview
evolution
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
evolution
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
evolution
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
evolution
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
evolution
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
evolution
the enzyme belongs to the glycoside hydrolase family 77, GH77
evolution
the enzyme belongs to the glycoside hydrolase family 77, GH77. The N-terminal domains of G77 members may represent a distinct type of starch-binding domain and define a distinct CBM family, which is supported by studying docking of maltooligosaccharides to the N-terminal domain in amylomaltases, representing the four clusters of the phylogenetic tree, preliminary evolutionary distribution of all 100 GH77 amylomaltases into four groups. sequence comparisons, overview
evolution
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
evolution
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
evolution
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
evolution
-
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. The N-terminal domains of G77 members may represent a distinct type of starch-binding domain and define a distinct CBM family, which is supported by studying docking of maltooligosaccharides to the N-terminal domain in amylomaltases, representing the four clusters of the phylogenetic tree, preliminary evolutionary distribution of all 100 GH77 amylomaltases into four groups, sequence comparisons, overview
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
-
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
-
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. The N-terminal domains of G77 members may represent a distinct type of starch-binding domain and define a distinct CBM family, which is supported by studying docking of maltooligosaccharides to the N-terminal domain in amylomaltases, representing the four clusters of the phylogenetic tree, preliminary evolutionary distribution of all 100 GH77 amylomaltases into four groups. sequence comparisons, overview
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
-
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
-
evolution
-
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. The N-terminal domains of G77 members may represent a distinct type of starch-binding domain and define a distinct CBM family, which is supported by studying docking of maltooligosaccharides to the N-terminal domain in amylomaltases, representing the four clusters of the phylogenetic tree, preliminary evolutionary distribution of all 100 GH77 amylomaltases into four groups, sequence comparisons, overview
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
-
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
-
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
-
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
-
evolution
-
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. The N-terminal domains of G77 members may represent a distinct type of starch-binding domain and define a distinct CBM family, which is supported by studying docking of maltooligosaccharides to the N-terminal domain in amylomaltases, representing the four clusters of the phylogenetic tree, preliminary evolutionary distribution of all 100 GH77 amylomaltases into four groups, sequence comparisons, overview
-
evolution
-
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
-
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. The N-terminal domains of G77 members may represent a distinct type of starch-binding domain and define a distinct CBM family, which is supported by studying docking of maltooligosaccharides to the N-terminal domain in amylomaltases, representing the four clusters of the phylogenetic tree, preliminary evolutionary distribution of all 100 GH77 amylomaltases into four groups, sequence comparisons, overview
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
-
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. The N-terminal domains of G77 members may represent a distinct type of starch-binding domain and define a distinct CBM family, which is supported by studying docking of maltooligosaccharides to the N-terminal domain in amylomaltases, representing the four clusters of the phylogenetic tree, preliminary evolutionary distribution of all 100 GH77 amylomaltases into four groups, sequence comparisons, overview
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
-
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. The N-terminal domains of G77 members may represent a distinct type of starch-binding domain and define a distinct CBM family, which is supported by studying docking of maltooligosaccharides to the N-terminal domain in amylomaltases, representing the four clusters of the phylogenetic tree, preliminary evolutionary distribution of all 100 GH77 amylomaltases into four groups, sequence comparisons, overview
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
-
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
-
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
-
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
-
evolution
-
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. The N-terminal domains of G77 members may represent a distinct type of starch-binding domain and define a distinct CBM family, which is supported by studying docking of maltooligosaccharides to the N-terminal domain in amylomaltases, representing the four clusters of the phylogenetic tree, preliminary evolutionary distribution of all 100 GH77 amylomaltases into four groups, sequence comparisons, overview
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
-
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
-
evolution
-
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
-
evolution
Pyrobaculum calidifontis DSM 21063
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
Pyrobaculum calidifontis DSM 21063
-
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
-
evolution
Pyrobaculum calidifontis DSM 21063
-
the enzyme belongs to the glycoside hydrolase family 77, GH77
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
-
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
-
evolution
Corynebacterium glutamicum CCUG 27702
-
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
-
evolution
Corynebacterium glutamicum CCUG 27702
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. The N-terminal domains of G77 members may represent a distinct type of starch-binding domain and define a distinct CBM family, which is supported by studying docking of maltooligosaccharides to the N-terminal domain in amylomaltases, representing the four clusters of the phylogenetic tree, preliminary evolutionary distribution of all 100 GH77 amylomaltases into four groups, sequence comparisons, overview
-
evolution
Corynebacterium glutamicum CCUG 27702
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
Corynebacterium glutamicum NBRC 12168
-
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
-
evolution
Corynebacterium glutamicum NBRC 12168
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. The N-terminal domains of G77 members may represent a distinct type of starch-binding domain and define a distinct CBM family, which is supported by studying docking of maltooligosaccharides to the N-terminal domain in amylomaltases, representing the four clusters of the phylogenetic tree, preliminary evolutionary distribution of all 100 GH77 amylomaltases into four groups, sequence comparisons, overview
-
evolution
Corynebacterium glutamicum NBRC 12168
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
Corynebacterium glutamicum NRRL B-2784
-
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
-
evolution
Corynebacterium glutamicum NRRL B-2784
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. The N-terminal domains of G77 members may represent a distinct type of starch-binding domain and define a distinct CBM family, which is supported by studying docking of maltooligosaccharides to the N-terminal domain in amylomaltases, representing the four clusters of the phylogenetic tree, preliminary evolutionary distribution of all 100 GH77 amylomaltases into four groups, sequence comparisons, overview
-
evolution
Corynebacterium glutamicum NRRL B-2784
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
-
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. The N-terminal domains of G77 members may represent a distinct type of starch-binding domain and define a distinct CBM family, which is supported by studying docking of maltooligosaccharides to the N-terminal domain in amylomaltases, representing the four clusters of the phylogenetic tree, preliminary evolutionary distribution of all 100 GH77 amylomaltases into four groups, sequence comparisons, overview
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
Pyrobaculum aerophilum CIP 104966
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
Pyrobaculum aerophilum CIP 104966
-
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview
-
evolution
Streptococcus agalactiae YZ1605
-
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
-
evolution
Thermus aquaticus ATCC 33923
-
members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. The N-terminal domains of G77 members may represent a distinct type of starch-binding domain and define a distinct CBM family, which is supported by studying docking of maltooligosaccharides to the N-terminal domain in amylomaltases, representing the four clusters of the phylogenetic tree, preliminary evolutionary distribution of all 100 GH77 amylomaltases into four groups. sequence comparisons, overview
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 77, GH77. The N-terminal domains of G77 members may represent a distinct type of starch-binding domain and define a distinct CBM family, which is supported by studying docking of maltooligosaccharides to the N-terminal domain in amylomaltases, representing the four clusters of the phylogenetic tree, preliminary evolutionary distribution of all 100 GH77 amylomaltases into four groups. sequence comparisons, overview
-
metabolism
key enzymes in the pathway for maltose catabolism. Glucose derived from the action of 4-alpha-glucanotransferase is subsequently metabolized via an Embden-Meyerhof pathway
metabolism
-
a distinct macroscopic debranching pathway is proposed: via 4-alpha-glucanotransferase, the G3-residue of the donor branch is transferred to a long (n >/= 5) linear Gn-residue linked to a different branching G residue
metabolism
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
metabolism
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
metabolism
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
metabolism
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
metabolism
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
metabolism
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
metabolism
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
metabolism
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
metabolism
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
metabolism
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
metabolism
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
metabolism
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism, involvement of amylomaltase in the degradation of glycogen in Escherichia coli
metabolism
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism. In Aquifex aeolicus, the enzyme might be involved in the metabolism of glycogen, since its gene is located in the glycogen operon and the bacterium lacks the gene for the maltose transport proteins
metabolism
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism. Amylomaltase may be involved in the synthesis of trehalose
metabolism
-
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
metabolism
-
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism. Amylomaltase may be involved in the synthesis of trehalose
-
metabolism
-
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
-
metabolism
-
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
-
metabolism
-
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
-
metabolism
-
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
-
metabolism
-
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
-
metabolism
-
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism. Amylomaltase may be involved in the synthesis of trehalose
-
metabolism
-
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
-
metabolism
-
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
-
metabolism
-
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
-
metabolism
-
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
-
metabolism
-
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
-
metabolism
-
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism, involvement of amylomaltase in the degradation of glycogen in Escherichia coli
-
metabolism
-
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism. Amylomaltase may be involved in the synthesis of trehalose
-
metabolism
-
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism. Amylomaltase may be involved in the synthesis of trehalose
-
metabolism
-
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism. Amylomaltase may be involved in the synthesis of trehalose
-
metabolism
-
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
-
metabolism
-
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
-
metabolism
-
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
-
metabolism
-
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
-
metabolism
-
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism. Amylomaltase may be involved in the synthesis of trehalose
-
metabolism
-
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
-
metabolism
Pyrobaculum calidifontis DSM 21063
-
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
-
metabolism
-
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
-
metabolism
Corynebacterium glutamicum CCUG 27702
-
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism. Amylomaltase may be involved in the synthesis of trehalose
-
metabolism
Corynebacterium glutamicum NBRC 12168
-
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism. Amylomaltase may be involved in the synthesis of trehalose
-
metabolism
Corynebacterium glutamicum NRRL B-2784
-
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism. Amylomaltase may be involved in the synthesis of trehalose
-
metabolism
-
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism. Amylomaltase may be involved in the synthesis of trehalose
-
metabolism
Pyrobaculum aerophilum CIP 104966
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amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
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metabolism
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amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism
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physiological function
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glycogen debranching enzyme (GDE) is bifunctional in that it exhibits both 4-alpha-glucanotransferase (EC 2.4.1.25) and amylo-alpha-1,6-glucosidase activity at two distinct catalytic sites. GDE converts the phosphorylase-limit biantennary branch into a linear maltooligosyl residue, which is then subjected to phosphorylase, and glycogen degradation continues
physiological function
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Presence of glucoamylase-resistant glucans among the products of the reaction of the Thermus thermophilus enzyme on amylose
physiological function
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
physiological function
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
physiological function
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
physiological function
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
physiological function
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
physiological function
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
physiological function
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
physiological function
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
physiological function
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
physiological function
in general, GH77 4-alpha-glucanotransferases catalyse transfer of a glucan chain from one alpha-1,4-glucan to extend another alpha-1,4-glucan or produce a cyclic alpha-1,4-glucan from a single linear alpha-1,4-glucan chain. The enzyme is also known as amylomaltase in prokaryotes and as disproportionating enzyme in plants
physiological function
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
physiological function
enzyme amylomaltase has the ability to synthesize cyclic glucans, or large ring cyclodextrins (LR-CDs), with a degree of polymerization (DP) of more than eight through intramolecular transglycosylation reaction. The LR-CDs are highly soluble in water and relatively have a larger hydrophobic cavity compared to the small ring cyclodextrin
physiological function
enzyme amylomaltase (AMM) from Thermus thermophilus is a thermo-active 4-alpha-glucanotransferase. It catalyzes the transfer of linear glucan segments from the donor amylose (AM) to the acceptor non-reducing end of the amylopectin (AP) chains via a disproportionation reaction. In a model starch system, AMM can in situ change starch fine molecular structure by elongating the AP chains at the expense of the length of AM chains resulting in significantly lower extent and rate of starch digestion
physiological function
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
physiological function
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
physiological function
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
physiological function
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
physiological function
in general, GH77 4-alpha-glucanotransferases catalyse transfer of a glucan chain from one alpha-1,4-glucan to extend another alpha-1,4-glucan or produce a cyclic alpha-1,4-glucan from a single linear alpha-1,4-glucan chain. The enzyme is also known as amylomaltase in prokaryotes and as disproportionating enzyme in plants
physiological function
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
physiological function
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
physiological function
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
physiological function
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
physiological function
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
physiological function
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
physiological function
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
physiological function
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
physiological function
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
physiological function
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
physiological function
in general, GH77 4-alpha-glucanotransferases catalyse transfer of a glucan chain from one alpha-1,4-glucan to extend another alpha-1,4-glucan or produce a cyclic alpha-1,4-glucan from a single linear alpha-1,4-glucan chain. The enzyme is also known as amylomaltase in prokaryotes and as disproportionating enzyme in plants
physiological function
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
physiological function
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
physiological function
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
physiological function
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
physiological function
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
physiological function
in general, GH77 4-alpha-glucanotransferases catalyse transfer of a glucan chain from one alpha-1,4-glucan to extend another alpha-1,4-glucan or produce a cyclic alpha-1,4-glucan from a single linear alpha-1,4-glucan chain. The enzyme is also known as amylomaltase in prokaryotes and as disproportionating enzyme in plants
physiological function
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
physiological function
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
physiological function
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Amylomaltase may be involved in the synthesis of trehalose in Corynebacterium glutamicum. The sugar is required by the bacterium to counteract osmotic stress and for the production of mycolic acids, important components of the cell envelope in Corynebacteriaceae
physiological function
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amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
physiological function
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enzyme amylomaltase has the ability to synthesize cyclic glucans, or large ring cyclodextrins (LR-CDs), with a degree of polymerization (DP) of more than eight through intramolecular transglycosylation reaction. The LR-CDs are highly soluble in water and relatively have a larger hydrophobic cavity compared to the small ring cyclodextrin
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physiological function
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4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
-
physiological function
-
in general, GH77 4-alpha-glucanotransferases catalyse transfer of a glucan chain from one alpha-1,4-glucan to extend another alpha-1,4-glucan or produce a cyclic alpha-1,4-glucan from a single linear alpha-1,4-glucan chain. The enzyme is also known as amylomaltase in prokaryotes and as disproportionating enzyme in plants
-
physiological function
-
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Amylomaltase may be involved in the synthesis of trehalose in Corynebacterium glutamicum. The sugar is required by the bacterium to counteract osmotic stress and for the production of mycolic acids, important components of the cell envelope in Corynebacteriaceae
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physiological function
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amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
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physiological function
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4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
-
physiological function
-
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
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physiological function
-
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
-
physiological function
-
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Presence of glucoamylase-resistant glucans among the products of the reaction of the Thermus thermophilus enzyme on amylose
-
physiological function
-
in general, GH77 4-alpha-glucanotransferases catalyse transfer of a glucan chain from one alpha-1,4-glucan to extend another alpha-1,4-glucan or produce a cyclic alpha-1,4-glucan from a single linear alpha-1,4-glucan chain. The enzyme is also known as amylomaltase in prokaryotes and as disproportionating enzyme in plants
-
physiological function
-
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
-
physiological function
-
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
-
physiological function
-
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
-
physiological function
-
enzyme amylomaltase has the ability to synthesize cyclic glucans, or large ring cyclodextrins (LR-CDs), with a degree of polymerization (DP) of more than eight through intramolecular transglycosylation reaction. The LR-CDs are highly soluble in water and relatively have a larger hydrophobic cavity compared to the small ring cyclodextrin
-
physiological function
-
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
-
physiological function
-
in general, GH77 4-alpha-glucanotransferases catalyse transfer of a glucan chain from one alpha-1,4-glucan to extend another alpha-1,4-glucan or produce a cyclic alpha-1,4-glucan from a single linear alpha-1,4-glucan chain. The enzyme is also known as amylomaltase in prokaryotes and as disproportionating enzyme in plants
-
physiological function
-
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Amylomaltase may be involved in the synthesis of trehalose in Corynebacterium glutamicum. The sugar is required by the bacterium to counteract osmotic stress and for the production of mycolic acids, important components of the cell envelope in Corynebacteriaceae
-
physiological function
-
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
-
physiological function
-
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
-
physiological function
-
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
-
physiological function
-
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
-
physiological function
-
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Presence of glucoamylase-resistant glucans among the products of the reaction of the Thermus thermophilus enzyme on amylose
-
physiological function
-
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
-
physiological function
-
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
-
physiological function
-
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
-
physiological function
-
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
-
physiological function
-
in general, GH77 4-alpha-glucanotransferases catalyse transfer of a glucan chain from one alpha-1,4-glucan to extend another alpha-1,4-glucan or produce a cyclic alpha-1,4-glucan from a single linear alpha-1,4-glucan chain. The enzyme is also known as amylomaltase in prokaryotes and as disproportionating enzyme in plants
-
physiological function
-
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
-
physiological function
-
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
-
physiological function
-
enzyme amylomaltase has the ability to synthesize cyclic glucans, or large ring cyclodextrins (LR-CDs), with a degree of polymerization (DP) of more than eight through intramolecular transglycosylation reaction. The LR-CDs are highly soluble in water and relatively have a larger hydrophobic cavity compared to the small ring cyclodextrin
-
physiological function
-
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
-
physiological function
-
in general, GH77 4-alpha-glucanotransferases catalyse transfer of a glucan chain from one alpha-1,4-glucan to extend another alpha-1,4-glucan or produce a cyclic alpha-1,4-glucan from a single linear alpha-1,4-glucan chain. The enzyme is also known as amylomaltase in prokaryotes and as disproportionating enzyme in plants
-
physiological function
-
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Amylomaltase may be involved in the synthesis of trehalose in Corynebacterium glutamicum. The sugar is required by the bacterium to counteract osmotic stress and for the production of mycolic acids, important components of the cell envelope in Corynebacteriaceae
-
physiological function
-
enzyme amylomaltase has the ability to synthesize cyclic glucans, or large ring cyclodextrins (LR-CDs), with a degree of polymerization (DP) of more than eight through intramolecular transglycosylation reaction. The LR-CDs are highly soluble in water and relatively have a larger hydrophobic cavity compared to the small ring cyclodextrin
-
physiological function
-
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
-
physiological function
-
in general, GH77 4-alpha-glucanotransferases catalyse transfer of a glucan chain from one alpha-1,4-glucan to extend another alpha-1,4-glucan or produce a cyclic alpha-1,4-glucan from a single linear alpha-1,4-glucan chain. The enzyme is also known as amylomaltase in prokaryotes and as disproportionating enzyme in plants
-
physiological function
-
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Amylomaltase may be involved in the synthesis of trehalose in Corynebacterium glutamicum. The sugar is required by the bacterium to counteract osmotic stress and for the production of mycolic acids, important components of the cell envelope in Corynebacteriaceae
-
physiological function
-
enzyme amylomaltase has the ability to synthesize cyclic glucans, or large ring cyclodextrins (LR-CDs), with a degree of polymerization (DP) of more than eight through intramolecular transglycosylation reaction. The LR-CDs are highly soluble in water and relatively have a larger hydrophobic cavity compared to the small ring cyclodextrin
-
physiological function
-
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
-
physiological function
-
in general, GH77 4-alpha-glucanotransferases catalyse transfer of a glucan chain from one alpha-1,4-glucan to extend another alpha-1,4-glucan or produce a cyclic alpha-1,4-glucan from a single linear alpha-1,4-glucan chain. The enzyme is also known as amylomaltase in prokaryotes and as disproportionating enzyme in plants
-
physiological function
-
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Amylomaltase may be involved in the synthesis of trehalose in Corynebacterium glutamicum. The sugar is required by the bacterium to counteract osmotic stress and for the production of mycolic acids, important components of the cell envelope in Corynebacteriaceae
-
physiological function
-
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
-
physiological function
-
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
-
physiological function
-
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Presence of glucoamylase-resistant glucans among the products of the reaction of the Thermus thermophilus enzyme on amylose
-
physiological function
-
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
-
physiological function
-
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
-
physiological function
-
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
-
physiological function
-
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
-
physiological function
-
enzyme amylomaltase has the ability to synthesize cyclic glucans, or large ring cyclodextrins (LR-CDs), with a degree of polymerization (DP) of more than eight through intramolecular transglycosylation reaction. The LR-CDs are highly soluble in water and relatively have a larger hydrophobic cavity compared to the small ring cyclodextrin
-
physiological function
-
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
-
physiological function
-
in general, GH77 4-alpha-glucanotransferases catalyse transfer of a glucan chain from one alpha-1,4-glucan to extend another alpha-1,4-glucan or produce a cyclic alpha-1,4-glucan from a single linear alpha-1,4-glucan chain. The enzyme is also known as amylomaltase in prokaryotes and as disproportionating enzyme in plants
-
physiological function
-
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Amylomaltase may be involved in the synthesis of trehalose in Corynebacterium glutamicum. The sugar is required by the bacterium to counteract osmotic stress and for the production of mycolic acids, important components of the cell envelope in Corynebacteriaceae
-
physiological function
-
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
-
physiological function
-
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
-
physiological function
-
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
-
physiological function
Pyrobaculum calidifontis DSM 21063
-
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
-
physiological function
Pyrobaculum calidifontis DSM 21063
-
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
-
physiological function
-
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
-
physiological function
-
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
-
physiological function
Corynebacterium glutamicum CCUG 27702
-
enzyme amylomaltase has the ability to synthesize cyclic glucans, or large ring cyclodextrins (LR-CDs), with a degree of polymerization (DP) of more than eight through intramolecular transglycosylation reaction. The LR-CDs are highly soluble in water and relatively have a larger hydrophobic cavity compared to the small ring cyclodextrin
-
physiological function
Corynebacterium glutamicum CCUG 27702
-
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
-
physiological function
Corynebacterium glutamicum CCUG 27702
-
in general, GH77 4-alpha-glucanotransferases catalyse transfer of a glucan chain from one alpha-1,4-glucan to extend another alpha-1,4-glucan or produce a cyclic alpha-1,4-glucan from a single linear alpha-1,4-glucan chain. The enzyme is also known as amylomaltase in prokaryotes and as disproportionating enzyme in plants
-
physiological function
Corynebacterium glutamicum CCUG 27702
-
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Amylomaltase may be involved in the synthesis of trehalose in Corynebacterium glutamicum. The sugar is required by the bacterium to counteract osmotic stress and for the production of mycolic acids, important components of the cell envelope in Corynebacteriaceae
-
physiological function
Corynebacterium glutamicum NBRC 12168
-
enzyme amylomaltase has the ability to synthesize cyclic glucans, or large ring cyclodextrins (LR-CDs), with a degree of polymerization (DP) of more than eight through intramolecular transglycosylation reaction. The LR-CDs are highly soluble in water and relatively have a larger hydrophobic cavity compared to the small ring cyclodextrin
-
physiological function
Corynebacterium glutamicum NBRC 12168
-
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
-
physiological function
Corynebacterium glutamicum NBRC 12168
-
in general, GH77 4-alpha-glucanotransferases catalyse transfer of a glucan chain from one alpha-1,4-glucan to extend another alpha-1,4-glucan or produce a cyclic alpha-1,4-glucan from a single linear alpha-1,4-glucan chain. The enzyme is also known as amylomaltase in prokaryotes and as disproportionating enzyme in plants
-
physiological function
Corynebacterium glutamicum NBRC 12168
-
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Amylomaltase may be involved in the synthesis of trehalose in Corynebacterium glutamicum. The sugar is required by the bacterium to counteract osmotic stress and for the production of mycolic acids, important components of the cell envelope in Corynebacteriaceae
-
physiological function
Corynebacterium glutamicum NRRL B-2784
-
enzyme amylomaltase has the ability to synthesize cyclic glucans, or large ring cyclodextrins (LR-CDs), with a degree of polymerization (DP) of more than eight through intramolecular transglycosylation reaction. The LR-CDs are highly soluble in water and relatively have a larger hydrophobic cavity compared to the small ring cyclodextrin
-
physiological function
Corynebacterium glutamicum NRRL B-2784
-
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
-
physiological function
Corynebacterium glutamicum NRRL B-2784
-
in general, GH77 4-alpha-glucanotransferases catalyse transfer of a glucan chain from one alpha-1,4-glucan to extend another alpha-1,4-glucan or produce a cyclic alpha-1,4-glucan from a single linear alpha-1,4-glucan chain. The enzyme is also known as amylomaltase in prokaryotes and as disproportionating enzyme in plants
-
physiological function
Corynebacterium glutamicum NRRL B-2784
-
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Amylomaltase may be involved in the synthesis of trehalose in Corynebacterium glutamicum. The sugar is required by the bacterium to counteract osmotic stress and for the production of mycolic acids, important components of the cell envelope in Corynebacteriaceae
-
physiological function
-
enzyme amylomaltase has the ability to synthesize cyclic glucans, or large ring cyclodextrins (LR-CDs), with a degree of polymerization (DP) of more than eight through intramolecular transglycosylation reaction. The LR-CDs are highly soluble in water and relatively have a larger hydrophobic cavity compared to the small ring cyclodextrin
-
physiological function
-
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
-
physiological function
-
in general, GH77 4-alpha-glucanotransferases catalyse transfer of a glucan chain from one alpha-1,4-glucan to extend another alpha-1,4-glucan or produce a cyclic alpha-1,4-glucan from a single linear alpha-1,4-glucan chain. The enzyme is also known as amylomaltase in prokaryotes and as disproportionating enzyme in plants
-
physiological function
-
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Amylomaltase may be involved in the synthesis of trehalose in Corynebacterium glutamicum. The sugar is required by the bacterium to counteract osmotic stress and for the production of mycolic acids, important components of the cell envelope in Corynebacteriaceae
-
physiological function
Pyrobaculum aerophilum CIP 104966
-
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
-
physiological function
Pyrobaculum aerophilum CIP 104966
-
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
-
physiological function
-
amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan
-
physiological function
Streptococcus agalactiae YZ1605
-
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
-
physiological function
Thermus aquaticus ATCC 33923
-
4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes
-
physiological function
-
in general, GH77 4-alpha-glucanotransferases catalyse transfer of a glucan chain from one alpha-1,4-glucan to extend another alpha-1,4-glucan or produce a cyclic alpha-1,4-glucan from a single linear alpha-1,4-glucan chain. The enzyme is also known as amylomaltase in prokaryotes and as disproportionating enzyme in plants
-
physiological function
-
in general, GH77 4-alpha-glucanotransferases catalyse transfer of a glucan chain from one alpha-1,4-glucan to extend another alpha-1,4-glucan or produce a cyclic alpha-1,4-glucan from a single linear alpha-1,4-glucan chain. The enzyme is also known as amylomaltase in prokaryotes and as disproportionating enzyme in plants
-
additional information
-
MQ-01 fails to exhibit mutagenic activity and does not display clastogenic properties in Chinese hamster lung fibroblast cells. In a 13-week subchronic toxicity study in rats, oral administration of MQ-01 at doses of up to 15 ml/kg body weight/day do not produce compound-related clinical signs or toxicity, changes in body weight gain, food consumption, hematology, clinical chemistry, urinalysis, organ weights, or in any gross and microscopic findings, overview
additional information
the amylomaltase from Escherichia coli, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Residue Tyr108 may be involved in alpha-glucan binding. Molecular docking, overview
additional information
analysis of the functional amino acid positions of Corynebacterium glutamicum amylomaltase (CgAM) involved in LR-CD synthesis, overview. Molecular interactions analysis using the three-dimensional crystal structure of enzyme CgAM (PDB ID 5B68), computational analysis
additional information
the amylomaltase from Corynebacterium glutamicum, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Molecular docking, overview
additional information
the catalytic triad residues of TaAM consist of D293, E340, and D395 as a nucleophile, acid-base catalyst, and transition state-stabilizer, respectively. Structure-function analysis, overview
additional information
the amylomaltase from Kushneria marisflavi, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Molecular docking, overview
additional information
the amylomaltase from Pelotomaculum thermopropionicum, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Molecular docking, overview
additional information
-
analysis of the functional amino acid positions of Corynebacterium glutamicum amylomaltase (CgAM) involved in LR-CD synthesis, overview. Molecular interactions analysis using the three-dimensional crystal structure of enzyme CgAM (PDB ID 5B68), computational analysis
-
additional information
-
the amylomaltase from Corynebacterium glutamicum, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Molecular docking, overview
-
additional information
-
the amylomaltase from Pelotomaculum thermopropionicum, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Molecular docking, overview
-
additional information
-
analysis of the functional amino acid positions of Corynebacterium glutamicum amylomaltase (CgAM) involved in LR-CD synthesis, overview. Molecular interactions analysis using the three-dimensional crystal structure of enzyme CgAM (PDB ID 5B68), computational analysis
-
additional information
-
the amylomaltase from Corynebacterium glutamicum, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Molecular docking, overview
-
additional information
-
the amylomaltase from Escherichia coli, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Residue Tyr108 may be involved in alpha-glucan binding. Molecular docking, overview
-
additional information
-
analysis of the functional amino acid positions of Corynebacterium glutamicum amylomaltase (CgAM) involved in LR-CD synthesis, overview. Molecular interactions analysis using the three-dimensional crystal structure of enzyme CgAM (PDB ID 5B68), computational analysis
-
additional information
-
the amylomaltase from Corynebacterium glutamicum, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Molecular docking, overview
-
additional information
-
analysis of the functional amino acid positions of Corynebacterium glutamicum amylomaltase (CgAM) involved in LR-CD synthesis, overview. Molecular interactions analysis using the three-dimensional crystal structure of enzyme CgAM (PDB ID 5B68), computational analysis
-
additional information
-
the amylomaltase from Corynebacterium glutamicum, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Molecular docking, overview
-
additional information
-
analysis of the functional amino acid positions of Corynebacterium glutamicum amylomaltase (CgAM) involved in LR-CD synthesis, overview. Molecular interactions analysis using the three-dimensional crystal structure of enzyme CgAM (PDB ID 5B68), computational analysis
-
additional information
-
the amylomaltase from Corynebacterium glutamicum, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Molecular docking, overview
-
additional information
-
analysis of the functional amino acid positions of Corynebacterium glutamicum amylomaltase (CgAM) involved in LR-CD synthesis, overview. Molecular interactions analysis using the three-dimensional crystal structure of enzyme CgAM (PDB ID 5B68), computational analysis
-
additional information
-
the amylomaltase from Corynebacterium glutamicum, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Molecular docking, overview
-
additional information
Corynebacterium glutamicum CCUG 27702
-
analysis of the functional amino acid positions of Corynebacterium glutamicum amylomaltase (CgAM) involved in LR-CD synthesis, overview. Molecular interactions analysis using the three-dimensional crystal structure of enzyme CgAM (PDB ID 5B68), computational analysis
-
additional information
Corynebacterium glutamicum CCUG 27702
-
the amylomaltase from Corynebacterium glutamicum, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Molecular docking, overview
-
additional information
Corynebacterium glutamicum NBRC 12168
-
analysis of the functional amino acid positions of Corynebacterium glutamicum amylomaltase (CgAM) involved in LR-CD synthesis, overview. Molecular interactions analysis using the three-dimensional crystal structure of enzyme CgAM (PDB ID 5B68), computational analysis
-
additional information
Corynebacterium glutamicum NBRC 12168
-
the amylomaltase from Corynebacterium glutamicum, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Molecular docking, overview
-
additional information
Corynebacterium glutamicum NRRL B-2784
-
analysis of the functional amino acid positions of Corynebacterium glutamicum amylomaltase (CgAM) involved in LR-CD synthesis, overview. Molecular interactions analysis using the three-dimensional crystal structure of enzyme CgAM (PDB ID 5B68), computational analysis
-
additional information
Corynebacterium glutamicum NRRL B-2784
-
the amylomaltase from Corynebacterium glutamicum, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Molecular docking, overview
-
additional information
-
analysis of the functional amino acid positions of Corynebacterium glutamicum amylomaltase (CgAM) involved in LR-CD synthesis, overview. Molecular interactions analysis using the three-dimensional crystal structure of enzyme CgAM (PDB ID 5B68), computational analysis
-
additional information
-
the amylomaltase from Corynebacterium glutamicum, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Molecular docking, overview
-
additional information
Thermus aquaticus ATCC 33923
-
the catalytic triad residues of TaAM consist of D293, E340, and D395 as a nucleophile, acid-base catalyst, and transition state-stabilizer, respectively. Structure-function analysis, overview
-
additional information
-
the amylomaltase from Pelotomaculum thermopropionicum, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Molecular docking, overview
-
additional information
-
the amylomaltase from Pelotomaculum thermopropionicum, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Molecular docking, overview
-
Show AA Sequence and Transmembrane Helices (17968 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
120000
174900
-
estimated from amino acid sequence, deduced from nucleotide sequence
53000
56000
57220
62000
64950
estimated from amino acid sequence, deduced from nucleotide sequence
71000
74000
81000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer or tetramer
homodimer
monomer
monomer or dimer
tetramer
additional information
dimer
the D-enzyme from Arabidopsis thaliana (AtDPE1) is present in a dimeric form
dimer
-
at pH 7.0, gel filtration and analytical sedimentation ultracentrifugation
dimer
-
at pH 7.0, gel filtration and analytical sedimentation ultracentrifugation
-
dimer or tetramer
-
at pH 5.5, gel filtration and analytical sedimentation ultracentrifugation
dimer or tetramer
the enzyme exists in two oligomeric states in solution, as a dimer and tetramer
dimer or tetramer
-
at pH 5.5, gel filtration and analytical sedimentation ultracentrifugation
-
monomer or dimer
the enzyme forms a dimer without NaCl and exists as a monomer in physiological concentration of NaCl
monomer or dimer
-
the enzyme forms a dimer without NaCl and exists as a monomer in physiological concentration of NaCl
-
tetramer
-
at pH 5.5-6.5 in presence of DMSO, gel filtration and analytical sedimentation ultracentrifugation
tetramer
-
at pH 5.5-6.5 in presence of DMSO, gel filtration and analytical sedimentation ultracentrifugation
-
additional information
DPE2 is a modular protein consisting of a family 77 glycosyl hydrolase domain, similar to DPE1, but unlike DPE1 the domain is interrupted by an insertion of about 150 amino acids as well as an N-terminal extension that consists of two carbohydrate binding modules, domain structure and functiosn, overview
additional information
the monomeric AtDPE1 possesses a long N-terminal part as a dimerization arm for engagement
additional information
the monomeric AtDPE1 possesses a long N-terminal part as a dimerization arm for engagement
additional information
isoform AtDPE2 specially contains two putative carbohydrate-binding modules (CBM20) at the N-terminus. In addition, the catalytic domain sequence is also divided into two parts as there is an insertion of 173 amino acid residues between the area of nucleophilic and acid/base-catalytic residues
additional information
isoform AtDPE2 specially contains two putative carbohydrate-binding modules (CBM20) at the N-terminus. In addition, the catalytic domain sequence is also divided into two parts as there is an insertion of 173 amino acid residues between the area of nucleophilic and acid/base-catalytic residues
additional information
the enzyme contains the domain N1, followed by the N-terminal domain (the potential novel SBD CBM family), the catalytic TIM-barrel domain A, and subdomains B1, B2 and B3, overview
additional information
-
the enzyme contains the domain N1, followed by the N-terminal domain (the potential novel SBD CBM family), the catalytic TIM-barrel domain A, and subdomains B1, B2 and B3, overview
-
additional information
-
the enzyme contains the domain N1, followed by the N-terminal domain (the potential novel SBD CBM family), the catalytic TIM-barrel domain A, and subdomains B1, B2 and B3, overview
-
additional information
-
the enzyme contains the domain N1, followed by the N-terminal domain (the potential novel SBD CBM family), the catalytic TIM-barrel domain A, and subdomains B1, B2 and B3, overview
-
additional information
Corynebacterium glutamicum CCUG 27702
-
the enzyme contains the domain N1, followed by the N-terminal domain (the potential novel SBD CBM family), the catalytic TIM-barrel domain A, and subdomains B1, B2 and B3, overview
-
additional information
-
the enzyme contains the domain N1, followed by the N-terminal domain (the potential novel SBD CBM family), the catalytic TIM-barrel domain A, and subdomains B1, B2 and B3, overview
-
additional information
-
the enzyme contains the domain N1, followed by the N-terminal domain (the potential novel SBD CBM family), the catalytic TIM-barrel domain A, and subdomains B1, B2 and B3, overview
-
additional information
-
the enzyme contains the domain N1, followed by the N-terminal domain (the potential novel SBD CBM family), the catalytic TIM-barrel domain A, and subdomains B1, B2 and B3, overview
-
additional information
Corynebacterium glutamicum NBRC 12168
-
the enzyme contains the domain N1, followed by the N-terminal domain (the potential novel SBD CBM family), the catalytic TIM-barrel domain A, and subdomains B1, B2 and B3, overview
-
additional information
-
the enzyme contains the domain N1, followed by the N-terminal domain (the potential novel SBD CBM family), the catalytic TIM-barrel domain A, and subdomains B1, B2 and B3, overview
-
additional information
Corynebacterium glutamicum NRRL B-2784
-
the enzyme contains the domain N1, followed by the N-terminal domain (the potential novel SBD CBM family), the catalytic TIM-barrel domain A, and subdomains B1, B2 and B3, overview
-
additional information
the enzyme contains the domain N1, followed by the N-terminal domain (the potential novel SBD CBM family), the catalytic TIM-barrel domain A, and subdomains B1, B2 and B3, overview
additional information
-
the enzyme contains the domain N1, followed by the N-terminal domain (the potential novel SBD CBM family), the catalytic TIM-barrel domain A, and subdomains B1, B2 and B3, overview
-
additional information
-
the tetramer shows a 4fold higher catalytic activity than the dimer
additional information
the structural lid, amino acids 99-97, at the active site generated by the tetramerization is closely associated with the bifunctionality and in particular with the alpha-1,4-transferase activity
additional information
-
the structural lid, amino acids 99-97, at the active site generated by the tetramerization is closely associated with the bifunctionality and in particular with the alpha-1,4-transferase activity
additional information
-
the tetramer shows a 4fold higher catalytic activity than the dimer
-
additional information
the three-dimensional structure of TaAM can be divided into two main domains, namely domain A and B. The subdomains B1, B2, and B3 are generated from insertion loops of (alpha,beta)8 barrel structure of domain A. Co-crystallization of TaAM with 34mer CA presents it as an asymmetric dimer. Domain structure, overview
additional information
Thermus aquaticus ATCC 33923
-
the three-dimensional structure of TaAM can be divided into two main domains, namely domain A and B. The subdomains B1, B2, and B3 are generated from insertion loops of (alpha,beta)8 barrel structure of domain A. Co-crystallization of TaAM with 34mer CA presents it as an asymmetric dimer. Domain structure, overview
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycolipoprotein
-
the enzyme is cell wall-associated via glycosylphosphatidylinositol anchoring
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis (PDB ID 1TZ7), structure comparisons, detailed overview
crystal structure analysis (PDB ID 5B68), structure comparisons, detailed overview
hanging drop vapor diffusion method, using 2.0 M ammonium sulfate and 0.1 M bis-tris methane (pH 6.5)
sitting drop vapor diffusion method, using 0.1 M bis-Tris pH 5.5 and 2.0 M ammonium sulfate
crystal structure analysis (PDB ID 4S3P), structure comparisons, detailed overview
TreX in complex with an acarbose ligand, microbatch method under oil at 18°C, dimeric crystal from 16% PEG 8000, 0.2 M NaCl, and 0.1 M CHES buffer, pH 9.5, tetrameric crystal form from 2.2 M ammonium phosphate and 0.1 M Tris-HCl buffer, pH 8.5. For the acarbose intermediate complex crystal, 0.1% acarbose is added to the protein, followed by incubation for 1 h prior to the setup of the crystal in 8% PEG 3000, 0.2M lithium sulfate, and 0.1 M imidazole buffer, pH 8.0, cyroprotection by 20% glycerol in mother liquor, in both crystal forms, the asymmetric unit consists of one dimer, X-ray diffraction structure determination and analysis at 2.8-3.0 A resolution
hanging-drop vapour-diffusion method. Crystal diffracts to 2.0 A resolution and belongs to space group C222(1), with unit-cell parameters a = 69.7, b = 120.3, c = 174.2 A
-
crystal structure analysis (PDB ID 6M6T), structure comparisons, detailed overview
crystallized in 2 forms, I and II, form I crystals belongs to hexagonal space group P6(4)22, form II crystals to orthorhombic space group P2(1)2(1)2
hanging drop vapor diffusion method at 25°C, crystal structure of the enzyme with and without an inhibitor, acarbose. The acarbose-bound structure clarifies that Glu123 and Asp214 are the catalytic nucleophile and acid/base catalyst, respectively
Gtase, hanging drop method, inhibitor complex,crystals belong to space group I222, unit-cell dimensions a = 92.6 A, b = 180.3 A, c = 199.2 A, free Gtase crystals a = 94.5 A, b = 181.4 A, c = 197.3 A
-
crystal structure analysis (PDB ID 1ESW), structure comparisons, detailed overview
crystals belong to space group P6(4) with cell parameters a = b = 154 A and c = 64 A
-
crystal structure analysis (PDB ID 2X1I), structure comparisons, detailed overview
to 2.3 A resolution. Structure shows a pattern of conformational flexibility in the 250s loop with higher B-factor. The conformational flexibility of the loop may be involved in substrate binding in the GH77 family
crystal structure analysis (PDB ID 1FP8), structure comparisons, detailed overview
purified recombinant enzyme, hanging drop vapour diffusion method, 0.003 ml of protein solution containing 10 mM MES-NaOH, pH 6.5, with 1 mM dithiothreitol is mixed with 0.001-0.003 ml of reservoir solution containing 0.4-0.8 M sodium malonate, pH 5.6, and 1 mM dithiothreitol, equilibration against reservoir solution at room temperature, 1 week, for enzyme-acarbose complexing the crystals are soaked in 0.5 ml of 0.8 M sodium malonate, pH 5.6, with 5 mg/ml acarbose and with or without and 4-deoxyglucose, for 30 min, X-ray diffraction structure determination and analysis at 1.9-2.5 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A406L
-
the mutant shows higher thermostability at 35-40°C, higher intermolecular transglucosylation activity with an upward shift in the optimum temperature and a slight increase in the optimum pH for disproportionation and cyclization reactions compared to the wild type enzyme. The mutant shows higher specific activities for starch transglucosylation (2.1fold) and disproportionation (1.4fold) than those of the wild type
A406V
A413F
site-directed mutagenesis, the mutant produces larger LR-CDs from CD36-CD40 as compared to CD29 by the wild-type, but with low yield. The A413F mutation affects the enzyme activities: starch tranglycosylation, disproportionation and cyclization
E231Y
site-directed mutagenesis, the E231Y mutant exhibits much higher kcat and Km values for starch transglycosylation, compared to that of the wild-type
G417F
site-directed mutagenesis, the mutant produces larger LR-CDs from CD36-CD40 as compared to CD29 by the wild-type, but with low yield. The G417F mutation hinders the enzyme's cyclization activity
H461A
the mutation leads to a significant (8.6fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate
H461D
the mutation leads to a significant (3.4fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate
H461R
the mutation leads to a significant (6fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate
H461S
the mutation leads to a significant (3.4fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate
H461W
the mutation leads to a significant (6fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate
N287Y
P228Y
site-directed mutagenesis, the mutant produces larger LR-CDs from CD36-CD40 as compared to CD29 by the wild-type. The P228Y mutation significantly lowers the kcat of disproportionation activity compared to wild-type
Y172A
Y23A
site-directed mutagenesis, the mutation affects the kinetic parameters of starch transglycosylation and cyclization
Y418A
-
the mutant shows a significant decrease in starch transglucosylation, disproportionation and cyclization activities compared to the wild type enzyme. The mutant produces large ring-cyclodextrins 36-40 from pea starch
Y418D
-
the mutant shows a significant decrease in starch transglucosylation, disproportionation and cyclization activities compared to the wild type enzyme. The mutant produces large ring-cyclodextrins 36-40 from pea starch
Y418F
-
the mutant shows a significant decrease in starch transglucosylation, disproportionation and cyclization activities compared to the wild type enzyme. The mutant produces large ring-cyclodextrins 29-33 from pea starch
Y418R
-
the mutant shows a significant decrease in starch transglucosylation, disproportionation and cyclization activities compared to the wild type enzyme. The mutant produces large ring-cyclodextrins 36-40 from pea starch
Y418S
-
the mutant shows a significant decrease in starch transglucosylation, disproportionation and cyclization activities compared to the wild type enzyme. The mutant produces large ring-cyclodextrins 36-40 from pea starch
Y418W
-
the mutant shows a significant decrease in starch transglucosylation, disproportionation and cyclization activities compared to the wild type enzyme. The mutant produces large ring-cyclodextrins 36-40 from pea starch
A413F
-
site-directed mutagenesis, the mutant produces larger LR-CDs from CD36-CD40 as compared to CD29 by the wild-type, but with low yield. The A413F mutation affects the enzyme activities: starch tranglycosylation, disproportionation and cyclization
-
E231Y
-
site-directed mutagenesis, the E231Y mutant exhibits much higher kcat and Km values for starch transglycosylation, compared to that of the wild-type
-
P228Y
-
site-directed mutagenesis, the mutant produces larger LR-CDs from CD36-CD40 as compared to CD29 by the wild-type. The P228Y mutation significantly lowers the kcat of disproportionation activity compared to wild-type
-
Y23A
-
site-directed mutagenesis, the mutation affects the kinetic parameters of starch transglycosylation and cyclization
-
A406L
-
the mutant shows higher thermostability at 35-40°C, higher intermolecular transglucosylation activity with an upward shift in the optimum temperature and a slight increase in the optimum pH for disproportionation and cyclization reactions compared to the wild type enzyme. The mutant shows higher specific activities for starch transglucosylation (2.1fold) and disproportionation (1.4fold) than those of the wild type
-
A406V
-
the mutant shows higher thermostability at 50°C, higher intermolecular transglucosylation activity with an upward shift in the optimum temperature and a slight increase in the optimum pH for disproportionation and cyclization reactions compared to the wild type enzyme. The mutant shows higher specific activities for starch transglucosylation (2.8fold) and disproportionation (2.1fold) than those of the wild type
-
A413F
-
site-directed mutagenesis, the mutant produces larger LR-CDs from CD36-CD40 as compared to CD29 by the wild-type, but with low yield. The A413F mutation affects the enzyme activities: starch tranglycosylation, disproportionation and cyclization
-
E231Y
-
site-directed mutagenesis, the E231Y mutant exhibits much higher kcat and Km values for starch transglycosylation, compared to that of the wild-type
-
N287Y
-
the mutant shows a significant decrease in all transglucosylation activities including starch transglucosylation, disproportionation, cyclization and coupling compared to the wild type enzyme, while hydrolysis activity is not changed. The mutant shows an increase in thermostability and substrate preference for maltoheptaose in addition to maltotriose
-
P228Y
-
site-directed mutagenesis, the mutant produces larger LR-CDs from CD36-CD40 as compared to CD29 by the wild-type. The P228Y mutation significantly lowers the kcat of disproportionation activity compared to wild-type
-
Y23A
-
site-directed mutagenesis, the mutation affects the kinetic parameters of starch transglycosylation and cyclization
-
A413F
-
site-directed mutagenesis, the mutant produces larger LR-CDs from CD36-CD40 as compared to CD29 by the wild-type, but with low yield. The A413F mutation affects the enzyme activities: starch tranglycosylation, disproportionation and cyclization
-
E231Y
-
site-directed mutagenesis, the E231Y mutant exhibits much higher kcat and Km values for starch transglycosylation, compared to that of the wild-type
-
P228Y
-
site-directed mutagenesis, the mutant produces larger LR-CDs from CD36-CD40 as compared to CD29 by the wild-type. The P228Y mutation significantly lowers the kcat of disproportionation activity compared to wild-type
-
Y23A
-
site-directed mutagenesis, the mutation affects the kinetic parameters of starch transglycosylation and cyclization
-
A413F
Corynebacterium glutamicum CCUG 27702
-
site-directed mutagenesis, the mutant produces larger LR-CDs from CD36-CD40 as compared to CD29 by the wild-type, but with low yield. The A413F mutation affects the enzyme activities: starch tranglycosylation, disproportionation and cyclization
-
E231Y
Corynebacterium glutamicum CCUG 27702
-
site-directed mutagenesis, the E231Y mutant exhibits much higher kcat and Km values for starch transglycosylation, compared to that of the wild-type
-
P228Y
Corynebacterium glutamicum CCUG 27702
-
site-directed mutagenesis, the mutant produces larger LR-CDs from CD36-CD40 as compared to CD29 by the wild-type. The P228Y mutation significantly lowers the kcat of disproportionation activity compared to wild-type
-
Y23A
Corynebacterium glutamicum CCUG 27702
-
site-directed mutagenesis, the mutation affects the kinetic parameters of starch transglycosylation and cyclization
-
A413F
-
site-directed mutagenesis, the mutant produces larger LR-CDs from CD36-CD40 as compared to CD29 by the wild-type, but with low yield. The A413F mutation affects the enzyme activities: starch tranglycosylation, disproportionation and cyclization
-
E231Y
-
site-directed mutagenesis, the E231Y mutant exhibits much higher kcat and Km values for starch transglycosylation, compared to that of the wild-type
-
H461A
-
the mutation leads to a significant (8.6fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate
-
H461D
-
the mutation leads to a significant (3.4fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate
-
H461R
-
the mutation leads to a significant (6fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate
-
H461S
-
the mutation leads to a significant (3.4fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate
-
H461W
-
the mutation leads to a significant (6fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate
-
P228Y
-
site-directed mutagenesis, the mutant produces larger LR-CDs from CD36-CD40 as compared to CD29 by the wild-type. The P228Y mutation significantly lowers the kcat of disproportionation activity compared to wild-type
-
Y23A
-
site-directed mutagenesis, the mutation affects the kinetic parameters of starch transglycosylation and cyclization
-
A413F
-
site-directed mutagenesis, the mutant produces larger LR-CDs from CD36-CD40 as compared to CD29 by the wild-type, but with low yield. The A413F mutation affects the enzyme activities: starch tranglycosylation, disproportionation and cyclization
-
E231Y
-
site-directed mutagenesis, the E231Y mutant exhibits much higher kcat and Km values for starch transglycosylation, compared to that of the wild-type
-
P228Y
-
site-directed mutagenesis, the mutant produces larger LR-CDs from CD36-CD40 as compared to CD29 by the wild-type. The P228Y mutation significantly lowers the kcat of disproportionation activity compared to wild-type
-
Y23A
-
site-directed mutagenesis, the mutation affects the kinetic parameters of starch transglycosylation and cyclization
-
A413F
-
site-directed mutagenesis, the mutant produces larger LR-CDs from CD36-CD40 as compared to CD29 by the wild-type, but with low yield. The A413F mutation affects the enzyme activities: starch tranglycosylation, disproportionation and cyclization
-
E231Y
-
site-directed mutagenesis, the E231Y mutant exhibits much higher kcat and Km values for starch transglycosylation, compared to that of the wild-type
-
P228Y
-
site-directed mutagenesis, the mutant produces larger LR-CDs from CD36-CD40 as compared to CD29 by the wild-type. The P228Y mutation significantly lowers the kcat of disproportionation activity compared to wild-type
-
Y23A
-
site-directed mutagenesis, the mutation affects the kinetic parameters of starch transglycosylation and cyclization
-
A413F
Corynebacterium glutamicum NBRC 12168
-
site-directed mutagenesis, the mutant produces larger LR-CDs from CD36-CD40 as compared to CD29 by the wild-type, but with low yield. The A413F mutation affects the enzyme activities: starch tranglycosylation, disproportionation and cyclization
-
E231Y
Corynebacterium glutamicum NBRC 12168
-
site-directed mutagenesis, the E231Y mutant exhibits much higher kcat and Km values for starch transglycosylation, compared to that of the wild-type
-
P228Y
Corynebacterium glutamicum NBRC 12168
-
site-directed mutagenesis, the mutant produces larger LR-CDs from CD36-CD40 as compared to CD29 by the wild-type. The P228Y mutation significantly lowers the kcat of disproportionation activity compared to wild-type
-
Y23A
Corynebacterium glutamicum NBRC 12168
-
site-directed mutagenesis, the mutation affects the kinetic parameters of starch transglycosylation and cyclization
-
A413F
-
site-directed mutagenesis, the mutant produces larger LR-CDs from CD36-CD40 as compared to CD29 by the wild-type, but with low yield. The A413F mutation affects the enzyme activities: starch tranglycosylation, disproportionation and cyclization
-
E231Y
-
site-directed mutagenesis, the E231Y mutant exhibits much higher kcat and Km values for starch transglycosylation, compared to that of the wild-type
-
P228Y
-
site-directed mutagenesis, the mutant produces larger LR-CDs from CD36-CD40 as compared to CD29 by the wild-type. The P228Y mutation significantly lowers the kcat of disproportionation activity compared to wild-type
-
Y23A
-
site-directed mutagenesis, the mutation affects the kinetic parameters of starch transglycosylation and cyclization
-
A413F
Corynebacterium glutamicum NRRL B-2784
-
site-directed mutagenesis, the mutant produces larger LR-CDs from CD36-CD40 as compared to CD29 by the wild-type, but with low yield. The A413F mutation affects the enzyme activities: starch tranglycosylation, disproportionation and cyclization
-
E231Y
Corynebacterium glutamicum NRRL B-2784
-
site-directed mutagenesis, the E231Y mutant exhibits much higher kcat and Km values for starch transglycosylation, compared to that of the wild-type
-
P228Y
Corynebacterium glutamicum NRRL B-2784
-
site-directed mutagenesis, the mutant produces larger LR-CDs from CD36-CD40 as compared to CD29 by the wild-type. The P228Y mutation significantly lowers the kcat of disproportionation activity compared to wild-type
-
Y23A
Corynebacterium glutamicum NRRL B-2784
-
site-directed mutagenesis, the mutation affects the kinetic parameters of starch transglycosylation and cyclization
-
W229H
-
kcat/KM value of transglycosylation activity significantly decreases to about 15% of wild-type, kcat/Km value of hydrolysis activity changes little
D214N
the specific activity of the D214N mutant is decreased about 10000fold as compared with that of the wild-type enzyme
E123Q
-
the specific activity of the mutant enzyme toward maltotriose is about 15000fold lower than the specific activity of the wild-type enzyme
E129Q
-
the specific activity of the mutant enzyme is almost the same as that of the wild-type enzyme
D214N
-
the specific activity of the D214N mutant is decreased about 10000fold as compared with that of the wild-type enzyme
-
Y54A
Y54C
Y54D
Y54E
Y54F
Y54G
Y54H
Y54I
Y54K
Y54L
Y54M
Y54N
Y54P
Y54Q
Y54R
Y54S
Y54T
Y54V
Y54W
F251G
mutation results in significantly lower glucose production but increased maltose production from maltopentose substrates, showing an altered substrate-binding affinity
Q256G
mutation results in increased Km for maltotriose and a sharp decrease of the transglycosylation factor for maltose
W258G
mutant shows neither cyclization nor coupling activity, suggesting that residue Trp258 plays an essential role in all catalytic activities including hydrolysis and transglycosylation activities
D293A
site-directed mutagenesis of the active site nucleophile, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
D293N
site-directed mutagenesis of the active site nucleophile, the D293N mutation reduces the pH stability of the enzyme, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
D294S
site-directed mutagenesis, the mutant shows highly reduced kcat and reduced activity with malto-oligomers compared to the wild-type enzyme
D395A
site-directed mutagenesis of the active site transition stabilizer, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
D395N
site-directed mutagenesis of the active site transition stabilizer, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
E340A
site-directed mutagenesis of the active site general acid/base catalyst, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
E340Q
site-directed mutagenesis of the active site general acid/base catalyst, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
E758Q
the mutant shows highly reduced activity compared to the wild-type enzyme
F366L
site-directed mutagenesis, the mutant shows reduced kcat compared and reduced activity with malto-oligomers compared to the wild-type enzyme
D293A
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
site-directed mutagenesis of the active site nucleophile, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
-
D293N
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
site-directed mutagenesis of the active site nucleophile, the D293N mutation reduces the pH stability of the enzyme, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
-
D395N
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
site-directed mutagenesis of the active site transition stabilizer, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
-
E340A
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
site-directed mutagenesis of the active site general acid/base catalyst, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
-
E340Q
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
site-directed mutagenesis of the active site general acid/base catalyst, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
-
additional information
A406V
-
the mutant shows higher thermostability at 50°C, higher intermolecular transglucosylation activity with an upward shift in the optimum temperature and a slight increase in the optimum pH for disproportionation and cyclization reactions compared to the wild type enzyme. The mutant shows higher specific activities for starch transglucosylation (2.8fold) and disproportionation (2.1fold) than those of the wild type
A406V
site-directed mutagenesis, the mutant shows higher thermostability and gives higher amount of LR-CD products, in comparison to the wild-type enzyme
N287Y
-
the mutant shows a significant decrease in all transglucosylation activities including starch transglucosylation, disproportionation, cyclization and coupling compared to the wild type enzyme, while hydrolysis activity is not changed. The mutant shows an increase in thermostability and substrate preference for maltoheptaose in addition to maltotriose
N287Y
site-directed mutagenesis, the mutant exhibits a higher thermostability, a changed LR-CD profile, and an increased substrate preference for maltoheptaose (G5) compared to wild-type
Y172A
-
mutant exhibits lower disproportionation, cyclization, and hydrolysis activities than the wild-type. The kcat/Km of the disproportionation reaction for the Y172A enzyme is 2.8fold lower than that of wild-type. The Y172A enzyme shows a product pattern different from that of wild-type at a long incubation time. The principal large-ring cyclodextrin products of the Y172A mutant are a cycloamylose mixture with a degree of polymerization of 28 or 29
Y172A
site-directed mutagenesis, the mutation causes a shift of principal LR-CDs to the larger size products
Y54A
-
hydrolytic activity is 39% of the wild-type value, cyclization activity is 192% of the wild-type value
Y54A
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
Y54C
-
hydrolytic activity is 48% of the wild-type value, cyclization activity is 122% of the wild-type value
Y54C
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
Y54D
-
hydrolytic activity is 38% of the wild-type value, cyclization activity is 177% of the wild-type value
Y54D
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
Y54E
-
hydrolytic activity is 48% of the wild-type value, cyclization activity is 157% of the wild-type value
Y54E
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
Y54F
-
hydrolytic activity is 96% of the wild-type value, cyclization activity is 91% of the wild-type value
Y54F
B7A9X4
site-directed mutagenesis, the mutant shows increased coupling and disproportionation activities compared to the wild-type enzyme
Y54G
-
hydrolytic activity is 16% of the wild-type value, cyclization activity is 167% of the wild-type value
Y54G
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
Y54H
-
hydrolytic activity is 76% of the wild-type value, cyclization activity is 164% of the wild-type value
Y54H
B7A9X4
site-directed mutagenesis, the mutant shows increased coupling and reduced disproportionation activities compared to the wild-type enzyme
Y54I
-
hydrolytic activity is 33% of the wild-type value, cyclization activity is 157% of the wild-type value
Y54I
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
Y54K
-
hydrolytic activity is 99% of the wild-type value, cyclization activity is 176% of the wild-type value
Y54K
B7A9X4
site-directed mutagenesis, the mutant shows unaltered coupling but reduced disproportionation activities compared to the wild-type enzyme
Y54L
-
hydrolytic activity is 39% of the wild-type value, cyclization activity is 189% of the wild-type value
Y54L
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
Y54M
-
hydrolytic activity is 39% of the wild-type value, cyclization activity is 81% of the wild-type value
Y54M
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
Y54N
-
hydrolytic activity is 30% of the wild-type value, cyclization activity is 159% of the wild-type value
Y54N
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
Y54P
-
hydrolytic activity is 5% of the wild-type value, cyclization activity is 48% of the wild-type value
Y54P
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
Y54Q
-
hydrolytic activity is 70% of the wild-type value, cyclization activity is 168% of the wild-type value
Y54Q
B7A9X4
site-directed mutagenesis, the mutant shows unaltered coupling but reduced disproportionation activities compared to the wild-type enzyme
Y54R
-
hydrolytic activity is 70% of the wild-type value, cyclization activity is 200% of the wild-type value
Y54R
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
Y54S
-
hydrolytic activity is 38% of the wild-type value, cyclization activity is 186% of the wild-type value
Y54S
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
Y54T
-
hydrolytic activity is 22% of the wild-type value, cyclization activity is 149% of the wild-type value
Y54T
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
Y54V
-
hydrolytic activity is 29% of the wild-type value, cyclization activity is 160% of the wild-type value
Y54V
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
Y54W
-
hydrolytic activity is 20% of the wild-type value, cyclization activity is 95% of the wild-type value
Y54W
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
additional information
the glycosyl hydrolase domain alone provides disproportionating activity with a much higher affinity for short maltodextrins than the complete wild-type enzyme, while absence of the carbohydrate binding modules completely abolishes activity with large complex carbohydrates, reflecting the presumed function of DPE2 in vivo
additional information
-
an agtA knockout of Aspergillus niger shows an increased susceptibility towards the cell wall-disrupting compound, phenotypic characterization of CFW hypersensitive DELTAagtA strain and AgtA/AgtB overexpression strains, overview
additional information
generation of truncated mutant DELTA167 that exhibits no starch transglycosylation activity, indicating that the N-terminal domain of CgAM is necessary for enzyme activity. Mutants molecular dynamic simulations, overview. The wild-type enzyme exhibits cyclization specific activity at 0.0012 U/mg, while P228Y, E231Y and G417F mutants show the same level of specific activity at range 0.0007 0.0013 U/mg
additional information
-
generation of truncated mutant DELTA167 that exhibits no starch transglycosylation activity, indicating that the N-terminal domain of CgAM is necessary for enzyme activity. Mutants molecular dynamic simulations, overview. The wild-type enzyme exhibits cyclization specific activity at 0.0012 U/mg, while P228Y, E231Y and G417F mutants show the same level of specific activity at range 0.0007 0.0013 U/mg
-
additional information
-
generation of truncated mutant DELTA167 that exhibits no starch transglycosylation activity, indicating that the N-terminal domain of CgAM is necessary for enzyme activity. Mutants molecular dynamic simulations, overview. The wild-type enzyme exhibits cyclization specific activity at 0.0012 U/mg, while P228Y, E231Y and G417F mutants show the same level of specific activity at range 0.0007 0.0013 U/mg
-
additional information
-
generation of truncated mutant DELTA167 that exhibits no starch transglycosylation activity, indicating that the N-terminal domain of CgAM is necessary for enzyme activity. Mutants molecular dynamic simulations, overview. The wild-type enzyme exhibits cyclization specific activity at 0.0012 U/mg, while P228Y, E231Y and G417F mutants show the same level of specific activity at range 0.0007 0.0013 U/mg
-
additional information
Corynebacterium glutamicum CCUG 27702
-
generation of truncated mutant DELTA167 that exhibits no starch transglycosylation activity, indicating that the N-terminal domain of CgAM is necessary for enzyme activity. Mutants molecular dynamic simulations, overview. The wild-type enzyme exhibits cyclization specific activity at 0.0012 U/mg, while P228Y, E231Y and G417F mutants show the same level of specific activity at range 0.0007 0.0013 U/mg
-
additional information
-
generation of truncated mutant DELTA167 that exhibits no starch transglycosylation activity, indicating that the N-terminal domain of CgAM is necessary for enzyme activity. Mutants molecular dynamic simulations, overview. The wild-type enzyme exhibits cyclization specific activity at 0.0012 U/mg, while P228Y, E231Y and G417F mutants show the same level of specific activity at range 0.0007 0.0013 U/mg
-
additional information
-
generation of truncated mutant DELTA167 that exhibits no starch transglycosylation activity, indicating that the N-terminal domain of CgAM is necessary for enzyme activity. Mutants molecular dynamic simulations, overview. The wild-type enzyme exhibits cyclization specific activity at 0.0012 U/mg, while P228Y, E231Y and G417F mutants show the same level of specific activity at range 0.0007 0.0013 U/mg
-
additional information
-
generation of truncated mutant DELTA167 that exhibits no starch transglycosylation activity, indicating that the N-terminal domain of CgAM is necessary for enzyme activity. Mutants molecular dynamic simulations, overview. The wild-type enzyme exhibits cyclization specific activity at 0.0012 U/mg, while P228Y, E231Y and G417F mutants show the same level of specific activity at range 0.0007 0.0013 U/mg
-
additional information
Corynebacterium glutamicum NBRC 12168
-
generation of truncated mutant DELTA167 that exhibits no starch transglycosylation activity, indicating that the N-terminal domain of CgAM is necessary for enzyme activity. Mutants molecular dynamic simulations, overview. The wild-type enzyme exhibits cyclization specific activity at 0.0012 U/mg, while P228Y, E231Y and G417F mutants show the same level of specific activity at range 0.0007 0.0013 U/mg
-
additional information
-
generation of truncated mutant DELTA167 that exhibits no starch transglycosylation activity, indicating that the N-terminal domain of CgAM is necessary for enzyme activity. Mutants molecular dynamic simulations, overview. The wild-type enzyme exhibits cyclization specific activity at 0.0012 U/mg, while P228Y, E231Y and G417F mutants show the same level of specific activity at range 0.0007 0.0013 U/mg
-
additional information
Corynebacterium glutamicum NRRL B-2784
-
generation of truncated mutant DELTA167 that exhibits no starch transglycosylation activity, indicating that the N-terminal domain of CgAM is necessary for enzyme activity. Mutants molecular dynamic simulations, overview. The wild-type enzyme exhibits cyclization specific activity at 0.0012 U/mg, while P228Y, E231Y and G417F mutants show the same level of specific activity at range 0.0007 0.0013 U/mg
-
additional information
the expression level of the recombinant enzyme in Escherichia coli is not very high. Analysis of the mRNA of initial seven codons at the 5'-end of the gene reveals the presence of a hair pin like secondary structure. This secondary structure is removed by site-directed mutagenesis, without altering the amino acids, which results in enhanced expression of the cloned gene
additional information
Pyrobaculum calidifontis DSM 21063
-
the expression level of the recombinant enzyme in Escherichia coli is not very high. Analysis of the mRNA of initial seven codons at the 5'-end of the gene reveals the presence of a hair pin like secondary structure. This secondary structure is removed by site-directed mutagenesis, without altering the amino acids, which results in enhanced expression of the cloned gene
-
additional information
-
the expression level of the recombinant enzyme in Escherichia coli is not very high. Analysis of the mRNA of initial seven codons at the 5'-end of the gene reveals the presence of a hair pin like secondary structure. This secondary structure is removed by site-directed mutagenesis, without altering the amino acids, which results in enhanced expression of the cloned gene
-
additional information
-
the expression level of the recombinant enzyme in Escherichia coli is not very high. Analysis of the mRNA of initial seven codons at the 5'-end of the gene reveals the presence of a hair pin like secondary structure. This secondary structure is removed by site-directed mutagenesis, without altering the amino acids, which results in enhanced expression of the cloned gene
-
additional information
mutations in the N-terminal region result in a sharp increase in alpha-1,4-transferase activity and a reduced level of alpha-1,6-glucosidase activity, overview
additional information
-
mutations in the N-terminal region result in a sharp increase in alpha-1,4-transferase activity and a reduced level of alpha-1,6-glucosidase activity, overview
additional information
Therminus sp.
-
optimization of amylomaltase for the synthesis of alpha-arbutin derivatives as tyrosinase inhibitors. Incubation of AMase with the tapioca starch donor and an alpha- or beta-arbutin acceptor yields at least three glycoside products. AMase has higher disproportionation and cyclization activities but lower hydrolysis activity compared to CGTase
additional information
-
the starch-binding domains of Bacillus stearothermophilus ET1 CGTase (E and DE) are introduced into the C-terminus of TAalphaGT to enhance the starch utilizing activity. The chimeric enzymes, TAalphaGT-E and TAalphaGT-DE, show no difference in temperature optimum, transglycosylation activity, and amylolytic degradation pattern compared to TAalphaGT wild-type. However, TAalphaGT-DE exhibits the highest molar specific activity toward amylose. TAalphaGT-DE modifies amylopectin molecules by its disproportionating activities to produce modified amylopectin clusters (MW 1000001000000) and produces cyclo-amyloses with DP of 19 through 35 from amylose molecules
additional information
B7A9X4
the amino acid substitution at Y54 or Y101 for removing their aromatic side chain increases cyclization activity, intra-molecular transglycosylation reaction, but decreases disproportionation, coupling and hydrolytic activities, inter-molecular reactions
additional information
-
the amino acid substitution at Y54 or Y101 for removing their aromatic side chain increases cyclization activity, intra-molecular transglycosylation reaction, but decreases disproportionation, coupling and hydrolytic activities, inter-molecular reactions
additional information
-
the starch-binding domains of Bacillus stearothermophilus ET1 CGTase (E and DE) are introduced into the C-terminus of TAalphaGT to enhance the starch utilizing activity. The chimeric enzymes, TAalphaGT-E and TAalphaGT-DE, show no difference in temperature optimum, transglycosylation activity, and amylolytic degradation pattern compared to TAalphaGT wild-type. However, TAalphaGT-DE exhibits the highest molar specific activity toward amylose. TAalphaGT-DE modifies amylopectin molecules by its disproportionating activities to produce modified amylopectin clusters (MW 1000001000000) and produces cyclo-amyloses with DP of 19 through 35 from amylose molecules
-
additional information
-
enzymatic modification of rice starch to produce highly branched amylopectin and amylose using alpha-glucanotransferase and maltogenic amylase, overview
additional information
the deletion mutant DELTAN130 is unable to use glycogen but has high disproportionating activity with maltodextrins
additional information
in the crumb of fresh white wheat bread, starch is fully gelatinized. Its molecular and three-dimensional structure are major factors limiting the rate of its digestion. In situ modification of starch during bread making with starch-modifying enzymes (maltogenic amylase and amylomaltase) and analysis of the impact thereof on bread characteristics, starch retrogradation and digestibility, overview. Maltogenic amylase treatment increases the relative content of short amylopectin chains. This results in lower starch retrogradation and crumb firmness upon storage, and reduces extent (up to 18%) of in vitro starch digestion for fresh and stored breads. Amylomaltase only modestly shortens amylose chains and has no measurable impact on amylopectin structure. Modification with this enzyme leads to slower bread crumb firming but does not influence starch digestibility
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9
-
the recombinant enzyme maintains more than 80% of its activity at a temperature range of 50-80°C and a pH range of 5.0-9.0
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
35 - 40
-
at short incubation time for 15 min at 40°C, the remaining activity of the wild type enzyme is 39.5%, whereas for 30 min incubation, the activity remained is 15.2%. At 35°C for a longer incubation time of 3 h, the remaining activity of the wild type enzyme is 45%
35 - 45
-
the specific activity remaining after 10 min at 35°C for the wild type enzyme is 49.3% while that for mutant enzyme N287Y is 91.4%. At 40°C, no activity of the wild type enzyme is left after 10 min but mutant N287Y shows 34.3% remaining activity. At 45°C, the wild type loses all activity after 10 min incubation time while 28.6% of the activity of mutant N287Y still remains
37 - 42
-
D-enzyme, activity decreases rapidly above 37°C and is almost completely lost at 42°C
37 - 80
-
stable at 37°C, retains more than 90% of its maximum activity between 55-80°C, half-life of activity of about 3 h at 80°C
50
50 - 80
-
the recombinant enzyme maintains more than 80% of its activity at a temperature range of 50-80°C and a pH range of 5.0-9.0
60 - 70
-
the thermostability at 60-70°C in pH 6.0 potassium phosphate buffer, after 2 h of incubation time, shows approximately 70-80% remaining activity
70
80
85
90
95
85
B7A9X4
stable up to, retains 50% activity after incubation at 80°C for 24 h, loses all activity after incubation at 100°C for 10 min
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable to freezing, glycerol reduces activity and cannot be used to stabilize the enzyme at freezing temperatures
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DMSO
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stored in purification buffer, activity is stable for over 6 months
-
-80°C, purified recombinant enzyme, 20 mM sodium phosphate buffer containing 15% glycerol, pH 7.0, no decrease in acivity observed for 1 month
-
4°C, purified enzyme in buffer shows little or no loss of activity in 1 month
-
4°C, relatively stable at low temperatures, may be stored for many months in a cold room with relatively little loss of activity
-
4°C, stable in 20 mM bis-Tris-propane buffer, pH 6.5, containing 10% glycerol, no loss of activity over 6 months
-
4°C, stored as a suspension in 3.2 M ammonium sulfate, no significant loss of activity for at least 1 month
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE column chromatography and phenyl column chromatography
HisTrap affinity column chromatography
HisTrap column chromatography
iminodiacetic acid-Sepharose column chromatography and Superdex 200 gel filtration
native and recombinant enzyme
Ni HiTrap column chromatography and Superdex 75 gel filtration
Ni-NTA agarose column chromatography and Superdex S200 gel filtration
partial
recombinant enzyme
recombinant expression of His5-tagged enzyme in Escherichia coli strain Origami (DE3) by nickel affinity chromatography, dialysis, and ultrafiltration
-
recombinant His-tagged alpaGTase 2.9fold from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by heat treatment and nickel affinity chromatography, removal of the His-tag through cleavage with bovine thrombin
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain MC1061 by nickel affinity chromatography
-
recombinant His-tagged TsalphaGT from Escherichia coli strain MC1061 by nickel affinity chromatography to homogeneity
-
recombinant His6-tagged MalQ from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
recombinant wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
chromosomal gene cloned and expressed in Escherichia coli and Corynebacterium glutamicum
-
cloned into pTrc99A plasmid vector and expressed in Escherichia coli JM105
-
cloning from a fosmid library, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, real-time PCR enzyme expression analysis, recombinant expression of His5-tagged enzyme in Escherichia coli strain Origami (DE3)
-
expressed in Escherichia coli
expressed in Escherichia coli BL21 Star (DE3) One Shot cells
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
expression of His-tagged enzyme in Escherichia coli strain MC1061
-
expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
expression of wild-type and mutant enzymes in Escherichia coli, sequence comparison
gene B9H00_13155, DNA and amino acid sequence determmination and analysis, phylogenetic analysis and tree
gene malQ, DNA and amino acid sequence determination and analysis, phylogenetic tree, sequence comparisons, expression of the His6-tagged enzyme in Escherichia coli strain BL21 (DE3)
gene malQ, DNA and amino acid sequence determmination and analysis, phylogenetic analysis and tree
gene Pcal_0768, DNA and amino acid sequence determination and analysis, recombinant expression of soluble and active enzyme in Escherichia coli
gene treX, cloning from the trehalose biosynthesis gene cluster, expression of the His-tagged enzyme in Escherichia coli
-
genes agtA and agtB, DNA and amino acid sequence determination and analysis, phylogenetic tree, overexpression in Aspergillus niger strain MGG029, subcloning in Escherichia coli
-
genes for amylomaltase are part of the glycogen operon
genes of wild-type and mutant enzymes are coexpressed in Escherichia coli cells with GroELS, tRNA(AGA), and tRNA(AGG)
-
high-level expression of recombinant 4-alpha-glucanotransferase under control of the tac promoter is achieved in Escherichia coli
human glycogen debrancher gene assigned to chromosome 1p21, cloned and expressed in insect cells
-
putative gene identified in the genome
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3). Non-fusion and His-tagged wild-type CgAM show similar specific activity on starch transglycosylation
STA11, both cDNA and gDNA corresponding to the D-enzyme cloned
gene malQ, DNA and amino acid sequence determmination and analysis, phylogenetic analysis and tree
gene malQ, DNA and amino acid sequence determmination and analysis, phylogenetic analysis and tree
gene malQ, DNA and amino acid sequence determmination and analysis, phylogenetic analysis and tree
STA11, both cDNA and gDNA corresponding to the D-enzyme cloned
-
STA11, both cDNA and gDNA corresponding to the D-enzyme cloned
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
investigation of molecular characteristics, microstructures, and physicochemical properties of modified starch gels prepared from partial enzyme treatments of the corn and rice starch pastes. Unlike the native and partially modified normal starches, the native and partially modified waxy starches can not form gels strong enough for textural analysis after 24 h for gel setting. The partially modified normal starches show specific apparent amylose contents and maximum iodine absorption wavelength, as well as the tri-modal molecular weight profiles and flatter side-chain distributions. The partially modified normal starch gels possess fractured surfaces with discontinuous crystalline fibrous assembly, which result in more brittle, rigid, and resilient gels compared with the native gels
biotechnology
-
industrial production of cycloamylase with mutant enzyme Y54G, which shows high cyclization activity and low hydrolytic activity
food industry
medicine
nutrition
synthesis
additional information
food industry
TmalphaGT can be used to produce granular corn starch, which contains amylose and amylopectin having lower molecular weights and a thermoreversible gelation property
food industry
-
thermostable 4-alpha-glucanotransferase from Thermus scotoductus is used for rice cake production
food industry
-
the disproportionating enzyme 4alphaGTase, is used to modify the structural properties of rice starch to produce a suitable fat substitute in reduced-fat mayonnaise. The mayonnaise fat is partially substituted with the 4alphaGTase-treated starch paste at levels up to 50% in combination with xanthan gum. All mayonnaises exhibit shear thinning behavior and yield stress. Viscoelastic properties of mayonnaise are altered, and the mayonnaises exhibited weak gel-like properties. The magnitude of elastic and loss moduli is also affected by 4alphaGTase-treated starch concentration and presence of xanthan gum, microstructure, method, overview
food industry
transglycosylation product maltosyl-alpha-(1->6)-mangiferin shows 5500fold higher aqueous solubility than mangiferin, and both maltosyl-alpha-(1->6)-mangiferin and glucosyl-alpha-(1->6)-mangiferin exhibits similar 1,1-diphenyl-2-picrylhydrazyl free radical scavenging activities compared to mangiferin
food industry
Parageobacillus galactosidasius DSM 18751
-
transglycosylation product maltosyl-alpha-(1->6)-mangiferin shows 5500fold higher aqueous solubility than mangiferin, and both maltosyl-alpha-(1->6)-mangiferin and glucosyl-alpha-(1->6)-mangiferin exhibits similar 1,1-diphenyl-2-picrylhydrazyl free radical scavenging activities compared to mangiferin
-
nutrition
B7A9X4
cycloamylose will be used in the food, pharmaceutical and chemical industries
nutrition
-
acting on gelatinized food-grade potato starch, PyAMase produced a thermoreversible starch product with gelatin-like properties. This thermoreversible gel has potential applications in the food industry
nutrition
-
acting on gelatinized food-grade potato starch, PyAMase produced a thermoreversible starch product with gelatin-like properties. This thermoreversible gel has potential applications in the food industry
-
synthesis
B7A9X4
cycloamylose will be used in the food, pharmaceutical and chemical industries
synthesis
-
the enzyme is useful in the enzymatic synthesis of dimaltosyl-beta-cyclodextrin via a transglycosylation reaction
synthesis
-
the recombinant enzyme is used to enzymatically-synthesized glycogen as a food ingredient
synthesis
-
development of an efficient biocatalytic production process of cycloamyloses directly from sucrose by use of Synechocystis sp. 4-alpha-glucanotransferase and Neisseria polysaccharea amylosucrase. From one-pot synthesis, the maximum cycloamylose yield of 9.6%, w/w with 0.3 M sucrose is achieved with 10 units/ml of amylosucrase and 0.1 unit/ml of 4-alpha-glucanotransferase at 40°C for a 3 h reaction in a simultaneous dual enzyme reaction mode. The size of linear alpha-(1,4)-glucan is positively related to the cycloamylose productivity by 4-alpha-glucanotransferase in a hyperbolic manner. The dual enzyme reaction converts sucrose directly to cycloamyloses via in situ transient linear alpha-(1,4)-glucan as an soluble intermediate
synthesis
-
combination of maltogenic amylase reactions from Bacillus stearothermophilus and 4-alpha-glucanotransferase from Thermus scotoductus to increase the water solubility of puerarin, an isoflavonoid derived from Radix puerariae. The puerarin transfer products, including maltosyl-alpha-(1->6)-puerarin as a major product, are reacted with alpha-glucanotransferase in the presence of amylose. The maltosyl-alpha-(1->6)-puerarin-cycloamylose complex is formed by an elongation reaction and cyclization by alpha-glucanotransferase. The encapsulation of puerarin or glycosylated puerarin with a macrocyclic amylose is widely applicable both to improving the water solubility of the compound and stabilizing it during cold storage
synthesis
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
synthesis
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
synthesis
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
synthesis
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
synthesis
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
synthesis
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
synthesis
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
synthesis
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
synthesis
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
synthesis
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
synthesis
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
synthesis
amylomaltase can be used to synthesize large ring cyclodextrins (LR-CDs), applied as drug solubilizer, gene delivery vehicle and protein aggregation suppressor. The enzyme has the ability to synthesize highly sought cyclic glucans, or large ring cyclodextrins (LR-CDs), with a degree of polymerization (DP) of more than eight through intramolecular transglycosylation reaction. The LR-CDs are highly soluble in water and relatively have a larger hydrophobic cavity compared to the small ring cyclodextrin
synthesis
-
erythritol-receptor products formed via AMase-catalyzed reactions, particularly maltotriosyl-erythritol (EG3), are promising prebiotic ingredients, with the prebiotic activity of erythritol derivatives being influenced by the length of the carbohydrate chain. Fermentation of EG3 results in the highest levels of lactic acid and total short-chain fatty acids, which may contribute to reduced pH levels
synthesis
Therminus sp.
-
synthesis of alpha-arbutin derivatives as tyrosinase (EC 1.14.18.1) inhibitors by engineered amylomaltase, production features comparison with cyclomaltodextrin glucanotransferase (CGTase, 2.4.1.19), overview. Incubation of AMase with the tapioca starch donor and an alpha- or beta-arbutin acceptor yields at least three glycoside products. AMase has higher disproportionation and cyclization activities but lower hydrolysis activity compared to CGTase
synthesis
recombinant Pcal_0768 is successfully employed in the synthesis of modified starch for producing thermo-reversible gel
synthesis
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
synthesis
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
synthesis
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
synthesis
-
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
synthesis
-
amylomaltase can be used to synthesize large ring cyclodextrins (LR-CDs), applied as drug solubilizer, gene delivery vehicle and protein aggregation suppressor. The enzyme has the ability to synthesize highly sought cyclic glucans, or large ring cyclodextrins (LR-CDs), with a degree of polymerization (DP) of more than eight through intramolecular transglycosylation reaction. The LR-CDs are highly soluble in water and relatively have a larger hydrophobic cavity compared to the small ring cyclodextrin
-
synthesis
-
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
-
synthesis
-
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
-
synthesis
-
the enzyme is useful in the enzymatic synthesis of dimaltosyl-beta-cyclodextrin via a transglycosylation reaction
-
synthesis
-
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
-
synthesis
-
recombinant Pcal_0768 is successfully employed in the synthesis of modified starch for producing thermo-reversible gel
-
synthesis
-
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
-
synthesis
-
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
-
synthesis
-
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
-
synthesis
-
amylomaltase can be used to synthesize large ring cyclodextrins (LR-CDs), applied as drug solubilizer, gene delivery vehicle and protein aggregation suppressor. The enzyme has the ability to synthesize highly sought cyclic glucans, or large ring cyclodextrins (LR-CDs), with a degree of polymerization (DP) of more than eight through intramolecular transglycosylation reaction. The LR-CDs are highly soluble in water and relatively have a larger hydrophobic cavity compared to the small ring cyclodextrin
-
synthesis
-
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
-
synthesis
-
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
-
synthesis
-
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
-
synthesis
-
recombinant Pcal_0768 is successfully employed in the synthesis of modified starch for producing thermo-reversible gel
-
synthesis
-
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
-
synthesis
-
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
-
synthesis
-
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
-
synthesis
-
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
-
synthesis
-
amylomaltase can be used to synthesize large ring cyclodextrins (LR-CDs), applied as drug solubilizer, gene delivery vehicle and protein aggregation suppressor. The enzyme has the ability to synthesize highly sought cyclic glucans, or large ring cyclodextrins (LR-CDs), with a degree of polymerization (DP) of more than eight through intramolecular transglycosylation reaction. The LR-CDs are highly soluble in water and relatively have a larger hydrophobic cavity compared to the small ring cyclodextrin
-
synthesis
-
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
-
synthesis
-
amylomaltase can be used to synthesize large ring cyclodextrins (LR-CDs), applied as drug solubilizer, gene delivery vehicle and protein aggregation suppressor. The enzyme has the ability to synthesize highly sought cyclic glucans, or large ring cyclodextrins (LR-CDs), with a degree of polymerization (DP) of more than eight through intramolecular transglycosylation reaction. The LR-CDs are highly soluble in water and relatively have a larger hydrophobic cavity compared to the small ring cyclodextrin
-
synthesis
-
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
-
synthesis
-
amylomaltase can be used to synthesize large ring cyclodextrins (LR-CDs), applied as drug solubilizer, gene delivery vehicle and protein aggregation suppressor. The enzyme has the ability to synthesize highly sought cyclic glucans, or large ring cyclodextrins (LR-CDs), with a degree of polymerization (DP) of more than eight through intramolecular transglycosylation reaction. The LR-CDs are highly soluble in water and relatively have a larger hydrophobic cavity compared to the small ring cyclodextrin
-
synthesis
-
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
-
synthesis
-
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
-
synthesis
-
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
-
synthesis
-
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
-
synthesis
-
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
-
synthesis
-
amylomaltase can be used to synthesize large ring cyclodextrins (LR-CDs), applied as drug solubilizer, gene delivery vehicle and protein aggregation suppressor. The enzyme has the ability to synthesize highly sought cyclic glucans, or large ring cyclodextrins (LR-CDs), with a degree of polymerization (DP) of more than eight through intramolecular transglycosylation reaction. The LR-CDs are highly soluble in water and relatively have a larger hydrophobic cavity compared to the small ring cyclodextrin
-
synthesis
-
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
-
synthesis
-
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
-
synthesis
Pyrobaculum calidifontis DSM 21063
-
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
-
synthesis
Pyrobaculum calidifontis DSM 21063
-
recombinant Pcal_0768 is successfully employed in the synthesis of modified starch for producing thermo-reversible gel
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synthesis
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starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
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synthesis
Corynebacterium glutamicum CCUG 27702
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amylomaltase can be used to synthesize large ring cyclodextrins (LR-CDs), applied as drug solubilizer, gene delivery vehicle and protein aggregation suppressor. The enzyme has the ability to synthesize highly sought cyclic glucans, or large ring cyclodextrins (LR-CDs), with a degree of polymerization (DP) of more than eight through intramolecular transglycosylation reaction. The LR-CDs are highly soluble in water and relatively have a larger hydrophobic cavity compared to the small ring cyclodextrin
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synthesis
Corynebacterium glutamicum CCUG 27702
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starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
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synthesis
Corynebacterium glutamicum NBRC 12168
-
amylomaltase can be used to synthesize large ring cyclodextrins (LR-CDs), applied as drug solubilizer, gene delivery vehicle and protein aggregation suppressor. The enzyme has the ability to synthesize highly sought cyclic glucans, or large ring cyclodextrins (LR-CDs), with a degree of polymerization (DP) of more than eight through intramolecular transglycosylation reaction. The LR-CDs are highly soluble in water and relatively have a larger hydrophobic cavity compared to the small ring cyclodextrin
-
synthesis
Corynebacterium glutamicum NBRC 12168
-
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
-
synthesis
Corynebacterium glutamicum NRRL B-2784
-
amylomaltase can be used to synthesize large ring cyclodextrins (LR-CDs), applied as drug solubilizer, gene delivery vehicle and protein aggregation suppressor. The enzyme has the ability to synthesize highly sought cyclic glucans, or large ring cyclodextrins (LR-CDs), with a degree of polymerization (DP) of more than eight through intramolecular transglycosylation reaction. The LR-CDs are highly soluble in water and relatively have a larger hydrophobic cavity compared to the small ring cyclodextrin
-
synthesis
Corynebacterium glutamicum NRRL B-2784
-
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
-
synthesis
-
amylomaltase can be used to synthesize large ring cyclodextrins (LR-CDs), applied as drug solubilizer, gene delivery vehicle and protein aggregation suppressor. The enzyme has the ability to synthesize highly sought cyclic glucans, or large ring cyclodextrins (LR-CDs), with a degree of polymerization (DP) of more than eight through intramolecular transglycosylation reaction. The LR-CDs are highly soluble in water and relatively have a larger hydrophobic cavity compared to the small ring cyclodextrin
-
synthesis
-
starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
-
synthesis
Pyrobaculum aerophilum CIP 104966
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starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
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synthesis
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starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview
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additional information
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
additional information
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
additional information
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
additional information
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
additional information
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
additional information
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
additional information
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
additional information
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
additional information
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
additional information
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
additional information
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
additional information
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
additional information
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
additional information
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
additional information
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
additional information
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potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
additional information
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potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
-
additional information
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potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
-
additional information
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potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
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additional information
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potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
-
additional information
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potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
-
additional information
-
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
-
additional information
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potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
-
additional information
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potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
-
additional information
-
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
-
additional information
-
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
-
additional information
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potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
-
additional information
-
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
-
additional information
-
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
-
additional information
-
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
-
additional information
-
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
-
additional information
-
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
-
additional information
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potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
-
additional information
-
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
-
additional information
-
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
-
additional information
-
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
-
additional information
-
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
-
additional information
-
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
-
additional information
Pyrobaculum calidifontis DSM 21063
-
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
-
additional information
-
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
-
additional information
Corynebacterium glutamicum CCUG 27702
-
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
-
additional information
Corynebacterium glutamicum NBRC 12168
-
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
-
additional information
Corynebacterium glutamicum NRRL B-2784
-
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
-
additional information
-
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
-
additional information
Pyrobaculum aerophilum CIP 104966
-
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
-
additional information
-
potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview
-
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