Information on EC 2.4.1.25 - 4-alpha-glucanotransferase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
2.4.1.25
-
RECOMMENDED NAME
GeneOntology No.
4-alpha-glucanotransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
show the reaction diagram
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
show the reaction diagram
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
O87172
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
show the reaction diagram
catalytic mechanism and domain structure and function
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
glycogen degradation I
-
glycogen degradation II
-
Metabolic pathways
-
Starch and sucrose metabolism
-
starch degradation II
-
starch degradation V
-
sucrose biosynthesis II
-
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).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4-alpha-glucanotransferase
-
-
4-alpha-glucanotransferase
-
-
4-alpha-glucanotransferase
-
-
4-alpha-GTase
-
-
4-alpha-GTase
-
-
4alphaGTase
-
-
4alphaGTase
-
-
alpha-1,4-transferase
P95868
-
alpha-amylase-like transglycosylase
-
-
alpha-glucanotransferase
-
-
alphaGTase
-
-
AMase
O87172
-
amylmaltase
O66937
-
amylmaltase
-
-
amylmaltase
Pyrobaculum aerophilum IM2
-
-
-
amylmaltase
O32462
-
amylomaltase
-
-
-
-
amylomaltase
-
-
amylomaltase
Q9LV91
-
amylomaltase
A6YM39
-
amylomaltase
Q9FDV9
-
amylomaltase
-
-
amylomaltase
Escherichia coli ML
-
-
-
amylomaltase
Q06801
-
amylomaltase
-
-
amylomaltase
Q60035
-
amylomaltase
O87172
-
amylomaltase
O87172
-
At2g40840
O22198
-
D-enzyme
-
-
-
-
D-enzyme
-
-
D-enzyme
-
-
debranching enzyme
-
-
debranching enzyme
-
;
-
debranching enzyme maltodextrin glycosyltransferase
-
-
-
-
dextrin glycosyltransferase
-
-
-
-
dextrin glycosyltransferase,
-
-
-
-
dextrin transglycosylase
-
-
-
-
disproportionating enzyme
-
-
-
-
disproportionating enzyme
O22198
-
disproportionating enzyme
-
-
disproportionating enzyme
-
-
disproportionating enzyme
-
-
EC 2.4.1.3
-
-
formerly
-
GH77 amylomaltase
A6YM39
-
glycogen debranching enzyme
-
-
glycogen debranching enzyme
-
-
glycogen debranching enzyme
-
-
maltodextrin glycosyltransferase
-
-
oligo-1,4-1,4-glucantransferase
-
-
oligo-1,4-1,4-glucantransferase
-
-
PyAMase
Pyrobaculum aerophilum IM2
-
-
-
TAalphaGT
-
-
TAalphaGT
Thermus aquaticus YT-1
-
-
-
TAalphaGTase
-
-
TmalphaGT
Q60035
-
TreX
-
enzyme displays isoamylase and 4-alpha-glucanotransferase activity
TS alpha GTase
-
-
TSalphaGT
-
-
maltodextrin glycosyltransferase
-
-
additional information
-
the enzyme belongs to the alpha-amylase family
additional information
A6YM39
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
-
GDE is a member of 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
O87172
the enzyme belongs to the glycoside hydrolase family 77, GH77, which belongs to the alpha-amylase superfamily, Clan H, together with GH13 and GH70
CAS REGISTRY NUMBER
COMMENTARY
9032-09-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
-
O22198
SwissProt
Manually annotated by BRENDA team
Columbia wild-type
-
-
Manually annotated by BRENDA team
strains CBS 513.88, NRRL3122, and N402, isozymes AgtA and AgtB encoded by genes agtA and agtB
-
-
Manually annotated by BRENDA team
Lyme disease spirochaete, strain BB0166, gene malQ
UniProt
Manually annotated by BRENDA team
bovine
-
-
Manually annotated by BRENDA team
37, TerBD20 and BAFR1; strain 137C
-
-
Manually annotated by BRENDA team
alpha-1,4-glucanotransferase gene, GenBank accession no.; D-enzyme sequence
GenBank
Manually annotated by BRENDA team
Chlamydomonas reinhardtii 137C
strain 137C
-
-
Manually annotated by BRENDA team
Clostridium butyricum NCIMB 7423
NCIMB 7423
-
-
Manually annotated by BRENDA team
IFO 3806; Ml 308; strain ML 30
-
-
Manually annotated by BRENDA team
strain ML
-
-
Manually annotated by BRENDA team
strain ML 30
-
-
Manually annotated by BRENDA team
Escherichia coli ML
ML
-
-
Manually annotated by BRENDA team
Escherichia coli ML
strain ML
-
-
Manually annotated by BRENDA team
Escherichia coli ML 30
strain ML 30
-
-
Manually annotated by BRENDA team
Escherichia coli ML 308
Ml 308
-
-
Manually annotated by BRENDA team
chicken
-
-
Manually annotated by BRENDA team
human
-
-
Manually annotated by BRENDA team
barley
-
-
Manually annotated by BRENDA team
sweet potato
-
-
Manually annotated by BRENDA team
L. cv. Laxton's progress No. 9; pea
-
-
Manually annotated by BRENDA team
Pseudomonas stutzeri NRRL B3389
NRRL B3389
-
-
Manually annotated by BRENDA team
Pyrobaculum aerophilum IM2
IM2
-
-
Manually annotated by BRENDA team
Pyrococcus sp. KOD1
KOD1
-
-
Manually annotated by BRENDA team
D-346, ATCC 56960; yeast
-
-
Manually annotated by BRENDA team
L.cv. May Queen; potato
SwissProt
Manually annotated by BRENDA team
potato
SwissProt
Manually annotated by BRENDA team
strain P2, gene treX
-
-
Manually annotated by BRENDA team
strain P2, gene treX
-
-
Manually annotated by BRENDA team
strain PCC 6803, ATCC 27184#
-
-
Manually annotated by BRENDA team
ATCC 33923
-
-
Manually annotated by BRENDA team
ATCC 33923, nucleotide sequence accession number, deposited in DDBJ/EMBL/GenBank
SwissProt
Manually annotated by BRENDA team
gene malQ
-
-
Manually annotated by BRENDA team
strain YT-1
-
-
Manually annotated by BRENDA team
Thermus aquaticus YT-1
strain YT-1
-
-
Manually annotated by BRENDA team
strain ATCC 27978
-
-
Manually annotated by BRENDA team
strain HB8
UniProt
Manually annotated by BRENDA team
cv. Hartog and cv. Axona
-
-
Manually annotated by BRENDA team
broad bean, L.major
-
-
Manually annotated by BRENDA team
maize
-
-
Manually annotated by BRENDA team
sweet corn
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
-
-
-
-
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
show the reaction diagram
-
-
-
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
show the reaction diagram
-
-
-
r
(alpha-1,4-D-glucan)m + H2O
(alpha-1,4-D-glucan)x + (alpha-1,4-D-glucan)m-x
show the reaction diagram
-
-
-
r
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
show the reaction diagram
O87172, -
-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
show the reaction diagram
-
-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
show the reaction diagram
-
-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
show the reaction diagram
-
-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
show the reaction diagram
Q06801
-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
show the reaction diagram
-
-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
show the reaction diagram
-
-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
show the reaction diagram
-
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
-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
show the reaction diagram
O22198
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
-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharide
show the reaction diagram
O22198
-
-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharide
show the reaction diagram
-
maltose and a highly branched, soluble heteroglycan are excellent substrates for DPE2
-
-
?
1,4-alpha-D-glucan + glucose
maltooligosaccharides
show the reaction diagram
O87172, -
-
-
?
1,4-alpha-D-glucan + glucose
maltooligosaccharides
show the reaction diagram
-
-
-
?
1,4-alpha-D-glucan + glucose
maltooligosaccharides
show the reaction diagram
-
-
-
?
1,4-alpha-D-glucan + glucose
maltooligosaccharides
show the reaction diagram
-
-
-
?
1,4-alpha-D-glucan + glucose
maltooligosaccharides
show the reaction diagram
Q06801
-
-
?
1,4-alpha-D-glucan + glucose
maltooligosaccharides
show the reaction diagram
-
-
-
?
1,4-alpha-D-glucan + glucose
maltooligosaccharides
show the reaction diagram
-
-
-
?
6-O-alpha-D-glucosyl-cyclodextrins + H2O
D-glucose + cyclodextrins
show the reaction diagram
-
-
-
?
6-O-alpha-D-glucosyl-cyclomalto-octaose + H2O
glucose + cyclodextrins
show the reaction diagram
-
-
-
?
6-O-alpha-D-glucosyl-cyclomaltoheptaose + H2O
D-glucose + cyclodextrins
show the reaction diagram
-
-
-
-
-
6-O-alpha-D-glucosyl-cyclomaltoheptaose + H2O
D-glucose + cyclodextrins
show the reaction diagram
-
-
-
?
64-O-alpha-maltooligosyl-pyridylamino-maltooctaose + maltohexaose
64-O-alpha-D-glucosyl-pyridylamino-maltooctaose + ?
show the reaction diagram
-
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
-
-
?
amylopectin + D-glucose
small oligosaccharides
show the reaction diagram
Q06801
-
without maltose
?
amylopectin + maltopentaose
maltooligosaccharides
show the reaction diagram
-
-
-
?
amylopectin + maltopentaose
maltooligosaccharides
show the reaction diagram
Q06801
-
-
?
amylopectin + maltopentaose
maltooligosaccharides
show the reaction diagram
-
-
-
?
amylopectin + maltopentaose
maltooligosaccharides
show the reaction diagram
-
-
-
?
amylopectin + maltopentaose
maltooligosaccharides
show the reaction diagram
-
-
-
?
amylopectin + maltose
?
show the reaction diagram
-
Gtase
-
-
?
amylose
cycloamylose
show the reaction diagram
-
the enzyme produces a cycloamylose with a minimum degree of polymerization of 16
-
-
?
amylose
?
show the reaction diagram
Thermus aquaticus, Thermus aquaticus YT-1
-
-
-
-
?
amylose + ?
cycloamylose + ?
show the reaction diagram
-
-
-
-
?
amylose + D-glucose
low molecular mass oligosaccharides
show the reaction diagram
Q06801
-
-
?
amylose + D-glucose
low molecular mass oligosaccharides
show the reaction diagram
-
-
-
?
amylose + D-glucose
low molecular mass oligosaccharides
show the reaction diagram
-
synthetic amylose AS-320
-
?
amylose + maltopentaose
maltooligosaccharides
show the reaction diagram
Q06801
-
-
?
amylose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
-
-
?
amylose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
-
-
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
show the reaction diagram
Q06801
-
-
-
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
show the reaction diagram
-
-
-
-
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
show the reaction diagram
O87172, -
-
cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
show the reaction diagram
-
-
cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
show the reaction diagram
-
-
cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
show the reaction diagram
-
-
cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
show the reaction diagram
-
-
cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
show the reaction diagram
-
-
cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
show the reaction diagram
-
-
cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
show the reaction diagram
-
-
cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
show the reaction diagram
-
-
cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
show the reaction diagram
-
-
cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
show the reaction diagram
-
-
cycloamylose
?
amylose + maltose
?
show the reaction diagram
-
Gtase
-
-
?
cycloamylose + D-glucose
?
show the reaction diagram
-
-
-
-
?
dodecyl-beta-maltoside + alpha-cyclodextrin
dodecyl-beta-maltooctaoside + ?
show the reaction diagram
-
-
-
-
?
dodecyl-beta-maltoside + starch
dodecyl-beta-maltooctaoside + ?
show the reaction diagram
-
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
-
-
?
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)
show the reaction diagram
-
i.e. B5/84 + G6PA
-
-
?
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
show the reaction diagram
-
-
-
-
?
glycogen + maltooligosaccharides
D-glucose + ?
show the reaction diagram
-
-
-
?
linear maltooligosaccharides + starch
?
show the reaction diagram
-, Q9FDV9
-
-
-
r
linear maltooligosaccharides + starch
?
show the reaction diagram
Chlamydomonas reinhardtii 137C
-
-
-
-
r
maltodextrin + D-glucose
maltooligosaccharides
show the reaction diagram
-
-
-
?
maltodextrin + maltodextrin
maltooligosaccharides
show the reaction diagram
Escherichia coli, Escherichia coli ML 308, Escherichia coli ML 30
-
-
-
?
maltodextrin + maltose
maltooligosaccharides + H2O
show the reaction diagram
-
-
-
?
maltodextrin + maltose
maltooligosaccharides + H2O
show the reaction diagram
Q06801
-
-
?
maltodextrin + maltose
maltooligosaccharides + H2O
show the reaction diagram
-
catabolic processing of glycogen and maltodextrins
-
?
maltodextrin + maltose
maltooligosaccharides + H2O
show the reaction diagram
Escherichia coli ML
-
-, catabolic processing of glycogen and maltodextrins
-
?
maltoheptaose + maltoheptaose
D-glucose + maltooligosaccharides
show the reaction diagram
Pyrobaculum aerophilum, Pyrobaculum aerophilum IM2
-
-
-
-
?
maltoheptaose + maltoheptaose
maltooligosaccharides
show the reaction diagram
-
-
-
-
?
maltoheptaose + maltoheptaose
?
show the reaction diagram
O87172, -
-
-
-
?
maltoheptaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
-
-
?
maltoheptaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
-
-
?
maltoheptaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
-
-
?
maltoheptaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
-
-
?
maltoheptaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
-
-
?
maltoheptaose + maltotriose
maltononaose + D-glucose
show the reaction diagram
-
D-enzyme
-
?
maltohexaose + maltodextrin
D-glucose + maltopentaose
show the reaction diagram
-
only amylomaltase, no polymers larger than the initial maltodextrin substrate, maltohexaose is a good donor substrate, but unable to function as an acceptor
-
?
maltohexaose + maltohexaose
D-glucose + maltooligosaccharides
show the reaction diagram
Pyrobaculum aerophilum, Pyrobaculum aerophilum IM2
-
-
-
-
?
maltohexaose + maltohexaose
maltooligosaccharides
show the reaction diagram
-
-
-
-
?
maltohexaose + maltohexaose
?
show the reaction diagram
O87172, -
-
-
-
?
maltohexaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
-
-
?
maltohexaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
-
-
?
maltohexaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
-
-
?
maltohexaose + maltotriose
maltodextrins
show the reaction diagram
-
-
-
-
?
maltohexaose + maltotriose
maltodextrins
show the reaction diagram
-
-
-
-
?
maltohexaose + maltotriose
maltodextrins
show the reaction diagram
-
-
-
-
?
maltohexaose + maltotriose
maltodextrins
show the reaction diagram
Pyrococcus sp. KOD1
-
-
-
-
?
maltohexaose + maltotriose
D-glucose + maltooligosaccharides
show the reaction diagram
-
-
-
?
maltononaose + maltotriose
maltoundecaose + D-glucose
show the reaction diagram
-
D-enzyme
-
?
maltooligosaccharides
maltooligosaccharides + D-glucose
show the reaction diagram
-
-
-
?
maltopentaitol
maltohexaitol + ?
show the reaction diagram
Escherichia coli, Escherichia coli ML 308, Escherichia coli ML 30
-
-
-
-
?
maltopentaose + maltodextrin
maltose + higher dextrins
show the reaction diagram
-
-
-
?
maltopentaose + maltopentaose
new oligosaccharides
show the reaction diagram
-
-
-
-
?
maltopentaose + maltopentaose
new oligosaccharides
show the reaction diagram
-
-
-
-
?
maltopentaose + maltopentaose
new oligosaccharides
show the reaction diagram
-
-
-
-
?
maltopentaose + maltopentaose
new oligosaccharides
show the reaction diagram
-
-
-
-
?
maltopentaose + maltopentaose
new oligosaccharides
show the reaction diagram
-
-
-
-
?
maltopentaose + maltopentaose
new oligosaccharides
show the reaction diagram
-
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
-
-
?
maltopentaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
-
-
-
?
maltopentaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
show the reaction diagram
Pseudomonas stutzeri NRRL B3389
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
D-glucose + maltooligosaccharides
show the reaction diagram
Pyrobaculum aerophilum, Pyrobaculum aerophilum IM2
-
-
-
-
?
maltopentaose + maltopentaose
?
show the reaction diagram
O87172, -
-
-
-
?
maltopentaose + maltotriose
maltoheptaose + D-glucose
show the reaction diagram
-
D-enzyme
-
?
maltopentaose + maltotriose
homologous 1,4-alpha-D-glucans
show the reaction diagram
-
amylomaltose
-
?
maltopentaose + maltotriose
maltodextrins
show the reaction diagram
-
-
-
?
maltopentaose + maltotriose
maltodextrins
show the reaction diagram
-
-
-
?
maltopentaose + maltotriose
maltodextrins
show the reaction diagram
Pyrococcus sp. KOD1
-
-
-
?
maltopentaose + maltotriose
D-glucose + maltooligosaccharides
show the reaction diagram
-
-
-
?
maltopentaose + maltotriose
D-glucose + maltooligosaccharides
show the reaction diagram
Q06801
-
-
?
maltose + (1,4-alpha-glucan)n+1
D-glucose + (1,4-alpha-glucan)n+1
show the reaction diagram
Escherichia coli, Escherichia coli ML
-
-
-
?
maltose + beta-cyclodextrin
6-O-alpha-maltosyl-beta-cyclodextrin
show the reaction diagram
-
condensation reaction mechanism, overview
mass spectrometric product identification
-
?
maltose + maltose
maltotriose + glucose
show the reaction diagram
-
-
-
-
?
maltose + maltose
maltotriose + glucose
show the reaction diagram
-
-
-
-
?
maltose + maltose
maltotriose + glucose
show the reaction diagram
-
-
-
-
r
maltose + maltose
maltotriose + glucose
show the reaction diagram
-
-
-
-
?
maltose + maltose
maltotriose + glucose
show the reaction diagram
-
key role in maltose metabolism
-
-
?
maltose + maltose
maltotriose + glucose
show the reaction diagram
Pseudomonas stutzeri, Pseudomonas stutzeri NRRL B3389
-
D-enzyme
-
-
?
maltose + maltose
maltotriose + glucose
show the reaction diagram
Pyrococcus sp. KOD1
-
-
-
-
?
maltose + maltose
maltotriose + glucose
show the reaction diagram
Escherichia coli ML
-
-
-
-
?
maltose + maltose
maltotriose + glucose
show the reaction diagram
Escherichia coli ML 30
-
-
-
-
?
maltose + maltose
maltooligosaccharides
show the reaction diagram
-
-
-
-
?
maltose + maltosyl-beta-cyclodextrin
?
show the reaction diagram
-
-
-
-
?
maltosyl-alpha-(1->6)-puerarin
?
show the reaction diagram
-
i.e. maltosyl-daidzein 8-C-glucoside
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
-
?
maltosylsucrose
?
show the reaction diagram
Escherichia coli, Escherichia coli ML 308, Escherichia coli ML 30
-
-
-
-
?
maltotetraitol
maltopentaitol + ?
show the reaction diagram
Escherichia coli, Escherichia coli ML 308, Escherichia coli ML 30
-
-
-
-
?
maltotetraose + maltodextrin
maltose + higher dextrins
show the reaction diagram
-
-
-
?
maltotetraose + maltopentaose
maltooligosaccharides
show the reaction diagram
Q06801
-
-
?
maltotetraose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
-
-
?
maltotetraose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
-
-
?
maltotetraose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
-
-
?
maltotetraose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
-
-
?
maltotetraose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
-
-
?
maltotetraose + maltotetraose
D-glucose + maltooligosaccharides
show the reaction diagram
Pyrobaculum aerophilum, Pyrobaculum aerophilum IM2
-
-
-
-
?
maltotetraose + maltotetraose
maltooligosaccharides
show the reaction diagram
-
-
-
-
?
maltotetraose + maltotetraose
?
show the reaction diagram
O87172, -
-
-
-
?
maltotetraose + maltotriose
glucose + maltoheptaose + maltodecaose
show the reaction diagram
-
D-enzyme
-
?
maltotetraose + maltotriose
homologous 1,4-alpha-glucans
show the reaction diagram
-
amylomaltose
-
?
maltotetraose + maltotriose
maltodextrins
show the reaction diagram
-
-
-
?
maltotetraose + maltotriose
maltodextrins
show the reaction diagram
-
-
-
?
maltotetraose + maltotriose
maltodextrins
show the reaction diagram
Q06801
-
-
?
maltotetraose + maltotriose
maltodextrins
show the reaction diagram
Pyrococcus sp. KOD1
-
-
-
?
maltotetraose + maltotriose
D-glucose + maltooligosaccharides
show the reaction diagram
-
-
-
?
maltotetraose + maltotriose
D-glucose + maltooligosaccharides
show the reaction diagram
-
-
-
?
maltotetraose + maltotriose
D-glucose + maltooligosaccharides
show the reaction diagram
Q06801
-
-
?
maltotetraose + maltotriose
D-glucose + maltooligosaccharides
show the reaction diagram
-
amylomaltose, most active with maltotetraose
-
?
maltotheptaose + maltotriose
maltodextrins
show the reaction diagram
-
-
-
-
?
maltotheptaose + maltotriose
maltodextrins
show the reaction diagram
-
-
-
-
?
maltotheptaose + maltotriose
maltodextrins
show the reaction diagram
-
-
-
-
?
maltotheptaose + maltotriose
maltodextrins
show the reaction diagram
Pyrococcus sp. KOD1
-
-
-
-
?
maltotheptaose + maltotriose
D-glucose + maltooligosaccharides
show the reaction diagram
-
-
-
?
maltotriose
maltooligosaccharides
show the reaction diagram
-
-
-
-
?
maltotriose
maltooligosaccharides
show the reaction diagram
Q2VJA0, -
-
-
-
?
maltotriose + acceptor
glucose + maltose + maltotetraose + maltopentaose + maltohexaose
show the reaction diagram
-
-
-
?
maltotriose + amylopectin
?
show the reaction diagram
-
-
-
-
?
maltotriose + maltodextrin
maltose + higher dextrins
show the reaction diagram
Pseudomonas stutzeri, Pseudomonas stutzeri NRRL B3389
-
-
-
?
maltotriose + maltodextrin
maltopentaose + ?
show the reaction diagram
Pseudomonas stutzeri, Pseudomonas stutzeri NRRL B3389
-
amylomaltase
-
?
maltotriose + maltotriose
maltopentaose + D-glucose
show the reaction diagram
-
-
-
?
maltotriose + maltotriose
maltopentaose + D-glucose
show the reaction diagram
-
-
-
?
maltotriose + maltotriose
maltopentaose + D-glucose
show the reaction diagram
-
-
-
?
maltotriose + maltotriose
maltopentaose + D-glucose
show the reaction diagram
-
-
-
?
maltotriose + maltotriose
maltopentaose + D-glucose
show the reaction diagram
-
D-enzyme
-
?
maltotriose + maltotriose
maltodextrins
show the reaction diagram
-
-
-
?
maltotriose + maltotriose
maltodextrins
show the reaction diagram
-
-
-
?
maltotriose + maltotriose
maltodextrins
show the reaction diagram
-
-
-
?
maltotriose + maltotriose
maltodextrins
show the reaction diagram
-
-
-
?
maltotriose + maltotriose
maltodextrins
show the reaction diagram
-
Mtase
-
?
maltotriose + maltotriose
D-glucose + maltooligosaccharides
show the reaction diagram
-
-
-
?
maltotriose + maltotriose
D-glucose + maltooligosaccharides
show the reaction diagram
Chlamydomonas reinhardtii, Chlamydomonas reinhardtii 137C
-
-
-
?
maltotriose + maltotriose
maltopentaose + maltotetraose
show the reaction diagram
-
-
-
?
maltotriose + maltotriose
maltopentaose + maltotetraose
show the reaction diagram
-
-
-
?
maltotriose + maltotriose
maltopentaose + maltotetraose
show the reaction diagram
-
-
-
?
maltotriose + maltotriose
D-glucose + maltopentaose + maltoheptaose + maltononaose + maltoundecaose
show the reaction diagram
-
D-enzyme
-
?
maltotriose + maltotriose
homologous alpha-1,4-D-glucans
show the reaction diagram
-
amylomaltose
-
?
maltotriose + maltotriose
D-glucose + maltopentaose
show the reaction diagram
-
-
-
-
?
maltotriose + maltotriose
maltooligosaccharides
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-beta-D-galactopyranoside + ?
?
show the reaction diagram
-
-
-
-
?
phi-dextrin
?
show the reaction diagram
-
-
-
-
?
starch + 2-deoxy-D-glucose
?
show the reaction diagram
Escherichia coli, Escherichia coli ML 308, Escherichia coli ML 30
-
-
-
-
?
starch + acceptor
glucose + maltose + other oligosaccharides
show the reaction diagram
-
-
-
?
starch + cellobiose
?
show the reaction diagram
-
-
-
-
?
starch + D-allose
oligosaccharides terminated by 4-O-alpha-D-glucopyranosyl-D-allose
show the reaction diagram
-
-
-
?
starch + D-glucosamine
?
show the reaction diagram
-
-
-
-
?
starch + D-glucose
low molecular mass oligosaccharides
show the reaction diagram
Q06801
-
-
?
starch + D-glucose
low molecular mass oligosaccharides
show the reaction diagram
-
-
-
?
starch + D-glucose
low molecular mass oligosaccharides
show the reaction diagram
-
soluble starch
-
?
starch + D-glucose
oligosaccharides
show the reaction diagram
Escherichia coli, Escherichia coli ML 308, Escherichia coli ML 30
-
-
-
?
starch + D-mannose
oligosaccharides terminated by 4-O-alpha-D-glucopyranosyl-D-mannose
show the reaction diagram
-
-
-
?
starch + D-sucrose
?
show the reaction diagram
-
-
-
-
?
starch + D-xylose
oligosaccharides terminated by 4-O-alpha-D-glucopyranosyl-D-xylose
show the reaction diagram
-
-
-
?
starch + isomaltose
?
show the reaction diagram
-
-
-
-
?
starch + L-sorbose
?
show the reaction diagram
-
-
-
-
?
starch + maltopentaose
alpha-1,4-D-glucans
show the reaction diagram
Q06801
-
-
?
starch + maltopentaose
alpha-1,4-D-glucans
show the reaction diagram
-
-
-
?
starch + maltopentaose
alpha-1,4-D-glucans
show the reaction diagram
-
-
-
?
starch + maltopentaose
alpha-1,4-D-glucans
show the reaction diagram
-
-
-
?
starch + maltopentaose
alpha-1,4-D-glucans
show the reaction diagram
-
starch can serve as acceptor molecule in glycosyl transfer reactions
-
?
starch + maltose
?
show the reaction diagram
-
Gtase
-
-
?
starch + methyl-alpha-D-glucoside
?
show the reaction diagram
Escherichia coli, Escherichia coli ML 308, Escherichia coli ML 30
-
-
-
-
?
starch + methyl-beta-D-glucoside
?
show the reaction diagram
-
-
-
-
?
starch + N-acetyl-D-glucosamine
oligosaccharides terminated by 4-O-alpha-D-glucopyranosyl-N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
?
starch + phenyl-alpha-D-glucoside
?
show the reaction diagram
-
-
-
-
?
starch + phenyl-beta-D-glucoside
?
show the reaction diagram
-
-
-
-
?
maltotriose + maltotriose
glucose + maltooligosaccharides
show the reaction diagram
O87172, -
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
2 different 4-alpha-glucanotransferases, MTAse and Gtase
-
-
-
additional information
?
-
-
glucose, maltose, maltotriose and maltotetraose are not acceptor molecules
-
-
-
additional information
?
-
-
glucose, maltose and maltotriose can act as acceptor, only maltotriose can act as donor
-
-
-
additional information
?
-
-
maltose is not a donor substrate, only weak acceptor activity
-
-
-
additional information
?
-
-
enzyme catalyzes not only intermolecular transglycosylation to produce linear alpha-1,4-glucan, but also intramolecular transglycosylation to produce cyclic alpha-1,4-glucan
-
-
-
additional information
?
-
-
glucose can only be used as acceptor of maltosyl units
-
-
-
additional information
?
-
-
2 major forms, D1 and D2
-
-
-
additional information
?
-
-
unable to use maltotriose as donor sugar or glucose as acceptor sugar
-
-
-
additional information
?
-
-
appears to be exclusively oligo-1,4-1,4-glucantransferase-amylo 1,6-glucosidase and does not have isoamylase, does not act on 6-O-alpha-maltosyl cyclomaltoheptaose
-
-
-
additional information
?
-
-
does not act on 6-O-alpha-maltosyl cyclomaltoheptaose
-
-
-
additional information
?
-
-
acts in concert with EC 2.4.1.1
-
-
-
additional information
?
-
-
acts in concert with EC 2.4.1.1
-
-
-
additional information
?
-
P0A4N1
acts in concert with EC 2.4.1.1
-
-
-
additional information
?
-
-
Gtase, glucose does not function as acceptor sugar, nor does it appear as reaction product
-
-
-
additional information
?
-
-
glucose is the major product of the D-enzyme reaction
-
-
-
additional information
?
-
Q06801
glucose is the major product of the D-enzyme reaction
-
-
-
additional information
?
-
-
glucose is the major product of the D-enzyme reaction
-
-
-
additional information
?
-
-
glucose is the major product of the D-enzyme reaction
-
-
-
additional information
?
-
-
glucose is the major product of the D-enzyme reaction
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
major pathway for starch degradation in chloroplasts
-
-
-
additional information
?
-
-
does not use maltose, maltotriose or maltotetraose as acceptor substrates in maltodextrinyltransfer reactions
-
-
-
additional information
?
-
-
maltose is inable to serve as a donor substrate, serving only as an acceptor substrate
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
D-glucosamine, N-acetyl-D-glucosamine and isomaltose have no activity as acceptors
-
-
-
additional information
?
-
-
maltose is not a product
-
-
-
additional information
?
-
Q06801
maltose is not a product
-
-
-
additional information
?
-
-
maltose is not a product
-
-
-
additional information
?
-
-
D-galactose, sugar alcohols such as sorbitol and xylitol and glycerol are not effective as acceptors
-
-
-
additional information
?
-
-
D-enzyme, maltohexaose is no initial substrate
-
-
-
additional information
?
-
-
amylopectin is no substrate, maltose is not a product
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
cannot use maltose or cyclohexaamylose as a substrate
-
-
-
additional information
?
-
-
2 glycosyltransferases, amylomaltase and D-enzyme
-
-
-
additional information
?
-
Q06801
maltose is no substrate
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
amylomaltase is involved in the conversion of maltose to sucrose in the cytosol
-
-
-
additional information
?
-
-
acting on gelatinized food-grade potato starch, PyAMase produced a thermoreversible starch product with gelatin-like properties
-
-
-
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
?
-
-
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
-
-
-
additional information
?
-
-
the smallest acceptor is glucose, the smallest donor is maltose
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
the enzyme reacts with small oligosaccharides, especially maltotriose, to form various maltooligosaccharides by using its disproportionating activity
-
-
-
additional information
?
-
-
4-alpha-glucanotransferase is essential for maltose metabolism in photosynthetic leaves
-
-
-
additional information
?
-
-
amylomaltase from Thermus aquaticus catalyzes three types of transglycosylation reaction, as well as a weak hydrolytic reaction of alpha-1,4 glucan
-
-
-
additional information
?
-
O87172
amylomaltases are capable of the synthesis of large cyclic glucans and the disproportionation of oligosaccharides
-
-
-
additional information
?
-
-
the enzyme is involved in glycogen metabolism by selective cleavage of the outer side chain
-
-
-
additional information
?
-
O87172, -
Thermus thermophilus AMase is among the most efficient 4-alpha-glucanotransferases in the alpha-amylase superfamily
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
O87172
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
-
-
-
additional information
?
-
A6YM39, -
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
-
-
-
additional information
?
-
-
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 75C, X-ray diffraction and relative crystallinity, overview
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
O87172, -
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
P95868, -
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
-
-
-
additional information
?
-
-
modification of rice starch by the enzyme
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
Thermus aquaticus YT-1
-
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
-
-
-
additional information
?
-
Pseudomonas stutzeri NRRL B3389
-
D-enzyme, maltohexaose is no initial substrate, 2 glycosyltransferases, amylomaltase and D-enzyme
-
-
-
additional information
?
-
Pyrobaculum aerophilum IM2
-
acting on gelatinized food-grade potato starch, PyAMase produced a thermoreversible starch product with gelatin-like properties
-
-
-
additional information
?
-
Escherichia coli ML
-
maltose is inable to serve as a donor substrate, serving only as an acceptor substrate
-
-
-
additional information
?
-
Escherichia coli ML 308
-
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
-
-
-
additional information
?
-
Escherichia coli ML 308
-
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, D-galactose, sugar alcohols such as sorbitol and xylitol and glycerol are not effective as acceptors
-
-
-
additional information
?
-
Clostridium butyricum NCIMB 7423
-
glucose, maltose and maltotriose can act as acceptor, only maltotriose can act as donor
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
the enzyme is involved in glycogen metabolism by selective cleavage of the outer side chain, 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
-
-
-
additional information
?
-
Escherichia coli ML 30
-
-
-
-
-
additional information
?
-
Escherichia coli ML 30
-
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
-
-
-
additional information
?
-
Escherichia coli ML 30
-
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, D-galactose, sugar alcohols such as sorbitol and xylitol and glycerol are not effective as acceptors
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
show the reaction diagram
-
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
-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
show the reaction diagram
O22198
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
-
-
?
maltodextrin + maltose
maltooligosaccharides + H2O
show the reaction diagram
Q06801
-
-
?
maltodextrin + maltose
maltooligosaccharides + H2O
show the reaction diagram
-
catabolic processing of glycogen and maltodextrins
-
?
maltopentaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
show the reaction diagram
Pseudomonas stutzeri NRRL B3389
-
metabolism of starch in the bacterium
-
?
additional information
?
-
-
amylomaltase is involved in the conversion of maltose to sucrose in the cytosol
-
-
-
additional information
?
-
-
4-alpha-glucanotransferase is essential for maltose metabolism in photosynthetic leaves
-
-
-
additional information
?
-
-
amylomaltase from Thermus aquaticus catalyzes three types of transglycosylation reaction, as well as a weak hydrolytic reaction of alpha-1,4 glucan
-
-
-
additional information
?
-
O87172
amylomaltases are capable of the synthesis of large cyclic glucans and the disproportionation of oligosaccharides
-
-
-
additional information
?
-
-
the enzyme is involved in glycogen metabolism by selective cleavage of the outer side chain
-
-
-
additional information
?
-
O87172, -
Thermus thermophilus AMase is among the most efficient 4-alpha-glucanotransferases in the alpha-amylase superfamily
-
-
-
additional information
?
-
-
the enzyme is involved in glycogen metabolism by selective cleavage of the outer side chain
-
-
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
D-enzyme, slight inhibition
acarbose
O87172, -
a strong mixed inhibitor with almost equal competitive and uncompetitive binding constants, acarbose is both bound in the active site and at another site
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
beta-cyclodextrin
-
a mixed-type inhibitor
cyclomaltohexaose
-
inhibition 25%
dithiothreitol
-
D-enzyme, slight inhibition
EDTA
-
D-enzyme, slight inhibition
Fe2+
-
D-enzyme, 50% inhibition
-
methyl-alpha-D-glucoside
-
competitive inhibition
Monoiodoacetic acid
-
-
p-chloromercuribenzoic acid
-
D-enzyme, 30% inhibition
p-chloromercuribenzoic acid
-
-
phenyl-beta-D-glucoside
-
competitive inhibition
Tris
-
D-enzyme, 50 mM, 35% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
alpha-cyclodextrin
-
activates GDE in liver
beta-cyclodextrin
-
activates GDE in liver
Cyclodextrin
-
the extent of 4-alpha-glucanotransferase activation increases with cyclodextrin concentration before reaching a constant value
-
DMSO
-
increases the enzyme's hydrolytic activity
gamma-cyclodextrin
-
activates GDE in liver
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%
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
10.5
-
6-O-alpha-D-glucosyl-cyclomaltoheptaose
-
native enzyme
11.2
-
6-O-alpha-D-glucosyl-cyclomaltoheptaose
-
recombinant enzyme
18
-
dodecyl-beta-maltoside
-
pH 5.2, 60C, 300 mM alpha-cyclodextrin
1.5
-
maltoheptaose
-
pH 6.7, 80C
5.7
-
maltoheptaose
-
pH 6.6, 70C
3.2
-
maltohexaose
-
pH 6.7, 80C
4.5
-
maltohexaose
-
pH 6.6, 70C
4.2
-
maltopentaose
-
pH 6.6, 70C
6.9
-
maltopentaose
-
pH 6.7, 80C
8.3
-
maltose
-
D-enzyme
71
-
maltose
-
pH 6.6, 70C
1.591
-
maltosyl-beta-cyclodextrin
-
pH 5.5, 75C
2.1
-
maltotetraose
-
pH 6.7, 80C
4.5
-
maltotetraose
-
pH 6.6, 70C
7.1
-
maltotetraose
-
-
2
-
maltotriose
Q2VJA0, -
wild-type, pH 6.0, 70C
3.3
-
maltotriose
-
-
3.7
-
maltotriose
-
pH 6.7, 80C
5.8
-
maltotriose
Q2VJA0, -
mutant F251G, pH 6.0, 70C
6.1
-
maltotriose
-
pH 6.6, 70C
7.3
-
maltotriose
-
-
9.5
-
maltotriose
Q2VJA0, -
mutant W258G, pH 6.0, 70C
12
-
maltotriose
-
-
12.9
-
maltotriose
-
mutant Y172A, pH 6.0, 30C
19.6
-
maltotriose
-
wild-type, pH 6.0, 30C
2.8
-
phi-dextrin
-
recombinant enzyme
-
3
-
phi-dextrin
-
native enzyme
-
165
-
maltotriose
Q2VJA0, -
mutant Q256G, pH 6.0, 70C
additional information
-
additional information
-
-
-
additional information
-
additional information
O87172, -
kinetics of wild-type and mutant enzymes at pH 6.5 and 70C, overview
-
additional information
-
additional information
O87172
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
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.99
-
maltoheptaose
O87172, -
pH 5.5, 70C, mutant D249S
8.7
-
maltoheptaose
-
pH 6.7, 80C
16
-
maltoheptaose
-
pH 6.6, 70C
159
-
maltoheptaose
O87172, -
pH 5.5, 70C, mutant F366L
213
-
maltoheptaose
O87172, -
pH 5.5, 70C, wild-type enzyme
3.26
-
maltohexaose
O87172, -
pH 5.5, 70C, mutant D249S
8.9
-
maltohexaose
-
pH 6.7, 80C
22
-
maltohexaose
-
pH 6.6, 70C
188
-
maltohexaose
O87172, -
pH 5.5, 70C, mutant F366L
304
-
maltohexaose
O87172, -
pH 5.5, 70C, wild-type enzyme
3.98
-
maltopentaose
O87172, -
pH 5.5, 70C, mutant D249S
22
-
maltopentaose
-
pH 6.6, 70C
24.8
-
maltopentaose
-
pH 6.7, 80C
179
-
maltopentaose
O87172, -
pH 5.5, 70C, mutant F366L
329
-
maltopentaose
O87172, -
pH 5.5, 70C, wild-type enzyme
1.3
-
maltose
-
pH 6.6, 70C
0.0113
-
maltosyl-beta-cyclodextrin
-
pH 5.5, 75C
0.97
-
maltotetraose
O87172, -
pH 5.5, 70C, mutant D249S
17
-
maltotetraose
-
pH 6.6, 70C
51.2
-
maltotetraose
-
pH 6.7, 80C
106
-
maltotetraose
O87172, -
pH 5.5, 70C, mutant F366L
425
-
maltotetraose
O87172, -
pH 5.5, 70C, wild-type enzyme
0.0017
-
maltotriose
Q2VJA0, -
mutant F251G, pH 6.0, 70C
0.005
-
maltotriose
Q2VJA0, -
mutant W258G, pH 6.0, 70C
0.015
-
maltotriose
Q2VJA0, -
wild-type, pH 6.0, 70C
0.036
-
maltotriose
-
mutant Y172A, pH 6.0, 30C
0.08
-
maltotriose
Q2VJA0, -
mutant Q256G, pH 6.0, 70C
0.157
-
maltotriose
-
wild-type, pH 6.0, 30C
0.68
-
maltotriose
O87172, -
pH 5.5, 70C, mutant D249S
18
-
maltotriose
-
pH 6.6, 70C
111
-
maltotriose
O87172, -
pH 5.5, 70C, mutant F366L
115
-
maltotriose
-
pH 6.7, 80C
317
-
maltotriose
O87172, -
pH 5.5, 70C, wild-type enzyme
additional information
-
additional information
-
-
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00035
-
maltotriose
Q2VJA0, -
mutant F251G, pH 6.0, 70C
12860
0.00048
-
maltotriose
Q2VJA0, -
mutant Q256G, pH 6.0, 70C; mutant W258G, pH 6.0, 70C
12860
0.0028
-
maltotriose
-
mutant Y172A, pH 6.0, 30C
12860
0.007
-
maltotriose
Q2VJA0, -
wild-type, pH 6.0, 70C
12860
0.0078
-
maltotriose
-
wild-type, pH 6.0, 30C
12860
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.003
-
acarbose
O87172, -
pH 5.5, 70C, competitive inhibition
0.004
-
acarbose
O87172, -
pH 5.5, 70C, uncompetitive inhibition
0.0556
-
beta-cyclodextrin
-
pH 5.5, 75C, recombinant His-tagged enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0027
-
O87172
mutant E758Q
1.36
-
-
-
2.9
-
O87172, -
-
5.19
-
O87172
wild-type enzyme
5.84
-
-
purified recombinant His-tagged enzyme
6.2
-
-
mutant Y172A, pH 6.0, 30C
21.8
-
-
wild-type, pH 6.0, 30C
47.5
-
Q06801
-
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
-
-
disproportionation and coupling activities of wild-type and Y54 mutated enzymes, overview
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.2
-
-
-
5.5
6
O87172, -
-
5.5
-
-
assay at
5.5
-
O87172, -
assay at
5.5
-
-
assay at
5.5
-
A6YM39, -
recombinant enzyme
5.5
-
-
assay at
5.5
-
P95868, -
assay at
6
-
-
assay at
7
-
-
recombinant enzyme
7.5
8
-
-
7.5
-
-
substrate: amylose
7.5
-
-
assay at
7.5
-
-
recombinant enzyme
7.5
-
-
recombinant enzyme
7.6
7.7
-
both amylomaltase and D-enzyme
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
7.5
O87172, -
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
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
D-enzyme
37
-
-
amylomaltase
37
-
Q06801
-
37
-
-
assay at
37
-
A6YM39, -
recombinant enzyme
37
-
-
assay at
40
-
P95868, -
assay at
45
-
-
recombinant enzyme
70
75
-
assay at
70
-
-
substrate: amylose
70
-
O87172, -
assay at
70
-
-
assay at
75
-
O87172, -
-
75
-
-
assay at
75
-
-
assay at
75
-
-
recombinant enzyme
75
-
-
recombinant enzyme
90
-
O66937
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50
90
O87172, -
-
60
100
-
60C: about 50% of maximal activity, 100C: about 30% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
the enzyme is present in the amyloplast of developing endosperm
Manually annotated by BRENDA team
-
kernel endosperm
Manually annotated by BRENDA team
-
pectoralis muscle; skeletal muscle
Manually annotated by BRENDA team
-
skeletal muscle
Manually annotated by BRENDA team
-
skeletal muscle
Manually annotated by BRENDA team
-
enzyme is more active in longissimus dorsi than in masseter. In both muscles the activity begins to fall at temperatures below 39C and is almost zero when the temperature decreases to below 15C. 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
Manually annotated by BRENDA team
-
germinating
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
51900
-
-
SDS-PAGE
53000
-
-
SDS-PAGE
54000
-
-
gel filtration
56000
-
-
size exclusion chromatography
57220
-
O87172, -
amino acid sequence
57220
-
-
calculated from sequence
59500
-
Q06801
native enzyme, SDS-PAGE
60000
-
Q06801
SDS-PAGE
62000
-
-
SDS-PAGE
64950
-
Q06801
estimated from amino acid sequence, deduced from nucleotide sequence
65000
-
Q06801
precursor, SDS-PAGE
70000
80000
-
sedimentation equilibrium
71000
-
-
gel filtration, low molecular weight form
71000
-
-
-
71000
-
-
strain ML 308
74000
-
-
amylomaltase, gel filtration
76690
-
-
calculated from cDNA
77880
-
-
calculated from cDNA
79000
-
-
SDS-PAGE
85000
-
-
SDS-PAGE
87000
-
-
gel filtration
93000
-
-
SDS-PAGE
98000
-
-
gel filtration
115000
-
-
D-enzyme, gel filtration
124000
-
-
strain Ml 30
134000
-
-
gel filtration
155000
-
-
sedimentation equilibrium
164000
-
-
high-speed sedimentation equilibrium
165000
-
-
purified recombinant enzyme, SDS-PAGE
166000
-
-
SDS-PAGE
170000
-
-
gel filtration
174900
-
-
estimated from amino acid sequence, deduced from nucleotide sequence
270000
-
-
approach-to-equilibrium method
370000
-
-
gel filtration, high molecular weight form
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 160000, SDS-PAGE
?
-
x * 83000, SDS-PAGE
?
-
x * 57969, calculated from sequence
?
O87172, -
x * 59337, sequence calculation
?
-
x * 57000, recombinant enzyme, SDS-PAGE
?
-
x * 81000, SDS-PAGE
?
Thermus aquaticus YT-1
-
x * 57969, calculated from sequence
-
dimer
-
1 * 38000 + 1 * 47000, amylomaltase; 1 * 52000 + 1 * 63000, D-enzyme
dimer
-
2 * 50000, SDS-PAGE
dimer
-
1 * 38000 + 1 * 47000, amylomaltase
dimer
-
2 * 79000, SDS-PAGE
dimer
-
at pH 7.0, gel filtration and analytical sedimentation ultracentrifugation
dimer
Pseudomonas stutzeri NRRL B3389
-
1 * 38000 + 1 * 47000, amylomaltase; 1 * 38000 + 1 * 47000, amylomaltase; 1 * 52000 + 1 * 63000, D-enzyme
-
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
P95868, -
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
-
1 * 120000, PAGE; 1 * 166000, SDS-PAGE
monomer
-
1 * 53000, SDS-PAGE
monomer
Q06801
1 * 60000, SDS-PAGE
monomer
-
1 * 85000, SDS-PAGE
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
-
the tetramer shows a 4fold higher catalytic activity than the dimer
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
P95868, -
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
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycolipoprotein
-
the enzyme is cell wall-associated via glycosylphosphatidylinositol anchoring
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-
TreX in complex with an acarbose ligand, microbatch method under oil at 18C, 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
P95868, -
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
-
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
-
crystals belong to space group P6(4) with cell parameters a = b = 154 A and c = 64 A
-
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
Q2VJA0, -
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
O87172
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
11
-
stable
3
8
-
loses 40% of the activity at pH 3.0, 80% at pH 8.0
4
10
O87172, -
-
4
7.5
O87172, -
pH stability of wild-type and mutant enzymes, overview
4
-
-
no activity detected
5
9
-
the recombinant enzyme maintains more than 80% of its activity at a temperature range of 50-80C and a pH range of 5.0-9.0
5.5
10
-
completely stable at 4C for 18 h
5.5
9
-
stable at 30C
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
quite stable at low temperatures
37
42
-
D-enzyme, activity decreases rapidly above 37C and is almost completely lost at 42C
37
80
-
stable at 37C, retains more than 90% of its maximum activity between 55-80C, half-life of activity of about 3 h at 80C
45
-
-
stable up to
50
80
-
the recombinant enzyme maintains more than 80% of its activity at a temperature range of 50-80C and a pH range of 5.0-9.0
50
-
-
amylomaltase, rapidly inactivated at temperatures above
50
-
-
10 min, almost complete loss of activity
60
-
-
loses activity when incubated for 10 min
70
-
-
stable below
80
-
-
30 min, less than 10% loss of activity
80
-
-
120 min, 10% loss of activity
80
-
O87172, -
stable up to at pH 5.5, half-life is 18 min
85
-
O87172, -
stable up to, retains 50% activity after incubation at 80C for 24 h, loses all activity after incubation at 100C for 10 min
85
-
-
210 min, 10fold decrease in activity
87
-
-
half-life: 506 min
89
-
-
half-life: 114 min
90
-
-
quite thermostable, retains full activity after 3 h
90
-
-
30 min, about 30% loss of activity
90
-
-
29 min, 10fold decrease in activity
95
-
-
half-life: 107 min
100
-
-
stable even after heating for 30 min
100
-
-
30 min, about 90% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
unstable to freezing, glycerol reduces activity and cannot be used to stabilize the enzyme at freezing temperatures
-
dithiothreitol decreases thermal stability of the enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, stable in 20 mM bis-Tris-propane buffer, pH 6.5, containing 10% glycerol, no loss of activity over 6 months
-
4C, very stable over long periods
-
4C, relatively stable at low temperatures, may be stored for many months in a cold room with relatively little loss of activity
-
-20C, stored in purification buffer, activity is stable for over 6 months
-
4C, purified enzyme in buffer shows little or no loss of activity in 1 month
-
0C, unstable to freezing
-
4C, stable for several months
-
4C, stored as a suspension in 3.2 M ammonium sulfate, no significant loss of activity for at least 1 month
-
-80C, purified recombinant enzyme, 20 mM sodium phosphate buffer containing 15% glycerol, pH 7.0, no decrease in acivity observed for 1 month
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant His6-tagged MalQ from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
A6YM39, -
E. coli ML 30, partially
-
both amylomaltase and D-enzyme
-
recombinant enzyme
-
native and recombinant enzyme
-
recombinant His-tagged enzyme from Escherichia coli strain MC1061 by nickel affinity chromatography
-
recombinant wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography
P95868, -
recombinant His-tagged alpaGTase 2.9fold from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
-
recombinant enzyme
-
native and recombinant enzyme
O87172, -
recombinant His-tagged enzyme by nickel affinity chromatography
-
recombinant His-tagged TsalphaGT from Escherichia coli strain MC1061 by nickel affinity chromatography to homogeneity
-
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
O87172
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
genes for amylomaltase are part of the glycogen operon
-
DPE2, phylogenetic analysis
-
expression 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
-
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)
A6YM39, -
putative gene identified in the genome
-
; STA11, both cDNA and gDNA corresponding to the D-enzyme cloned
-, Q9FDV9
STA11, both cDNA and gDNA corresponding to the D-enzyme cloned
-
gene MalQ cloned and expressed in Escherichia coli
-
expression in Escherichia coli
-
gene cloned an sequenced
-
expression in Escherichia coli
-
MalQ gene encodes amylomaltase
-
seuence determined
-
genes for amylomaltase are part of the glycogen operon
-
human glycogen debrancher gene assigned to chromosome 1p21, cloned and expressed in insect cells
-
putative gene identified in the genome
-
molecular cloning, sequencing and analysis of cDNA
-
expression in Escherichia coli
-
gene gtpK cloned, sequenced and overexpressed in Escherichia coli
-
cloned into pTrc99A plasmid vector and expressed in Escherichia coli JM105
-
YPR1184w gene encodes the glycogen debranching enzyme
-
cDNA clone isolated and expressed in Escherichia coli
Q06801
expressed in Escherichia coli MC1061 as a 6*His tagged protein
-
expression of His-tagged enzyme in Escherichia coli strain MC1061
-
expression of wild-type and mutant enzymes in Escherichia coli, sequence comparison
P95868, -
gene treX, cloning from the trehalose biosynthesis gene cluster, expression of the His-tagged enzyme in Escherichia coli
-
expression of His-tagged alpaGTase in Escherichia coli strain BL21 (DE3)
-
gene cloned, sequenced and expressed in Escherichia coli
-
Gtase gene cloned and expressed in Escherichia coli MV1184
-
chromosomal gene cloned and expressed in Escherichia coli and Corynebacterium glutamicum
-
cloned and expressed in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli strain BL21
-
; cloned and sequenced and overexpressed in Escherichia coli
O87172, -
expression in Escherichia coli
-
expression of His-tagged enzyme
-
gene malQ, expression in Bacillus subtilis strain NCIMB12378
-
overexpressed in Escherichia coli BL21
-
expression of His-tagged TsalphaGT in Escherichia coli strain MC1061
-
expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
O87172
malQ gene clone in pET expression vector system
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
Y54A
-
hydrolytic activity is 39% of the wild-type value, cyclization activity is 192% of the wild-type value
Y54A
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
F251G
Q2VJA0, -
mutation results in significantly lower glucose production but increased maltose production from maltopentose substrates, showing an altered substrate-binding affinity
Q256G
Q2VJA0, -
mutation results in increased Km for maltotriose and a sharp decrease of the transglycosylation factor for maltose
D293A
O87172, -
site-directed mutagenesis of the active site nucleophile, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
D293N
O87172, -
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
O87172, -
site-directed mutagenesis, the mutant shows highly reduced kcat and reduced activity with malto-oligomers compared to the wild-type enzyme
D395A
O87172, -
site-directed mutagenesis of the active site transition stabilizer, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
D395N
O87172, -
site-directed mutagenesis of the active site transition stabilizer, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
E340A
O87172, -
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
O87172, -
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
O87172
the mutant shows highly reduced activity 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
W229H
-
kcat/KM value of transglycosylation activity significantly decreases to about 15% of wild-type, kcat/Km value of hydrolysis activity changes little
additional information
P95868, -
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
-
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
-
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
Y54W
-
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
additional information
Thermus aquaticus YT-1
-
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
-
W258G
Q2VJA0, -
mutant shows neither cyclization nor coupling activity, suggesting that residue Trp258 plays an essential role in all catalytic activities including hydrolysis and transglycosylation activities
additional information
-
enzymatic modification of rice starch to produce highly branched amylopectin and amylose using alpha-glucanotransferase and maltogenic amylase, overview
F366L
O87172, -
site-directed mutagenesis, the mutant shows reduced kcat compared and reduced activity with malto-oligomers compared to the wild-type enzyme
additional information
O87172
the deletion mutant DELTAN130 is unable to use glycogen but has high disproportionating activity with maltodextrins
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
O66937
production of cycloamylose starch gels
medicine
O51188
lyme disease
medicine
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understanding of the molecular basis of Cori's disease
nutrition
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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
Pyrobaculum aerophilum IM2
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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
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synthesis
Q06801
production of cycloamylose
synthesis
-
the enzyme is useful in the enzymatic synthesis of dimaltosyl-beta-cyclodextrin via a transglycosylation reaction
synthesis
-
the enzyme is useful in the enzymatic synthesis of dimaltosyl-beta-cyclodextrin via a transglycosylation reaction
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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 40C 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
O32462
production of cycloamylose
food industry
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TmalphaGT can be used to produce granular corn starch, which contains amylose and amylopectin having lower molecular weights and a thermoreversible gelation property
synthesis
-
production of isomalto-oligosaccharides
analysis
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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
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industrial production of cycloamylase with mutant enzyme Y54G, which shows high cyclization activity and low hydrolytic activity
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
nutrition
O87172, -
cycloamylose will be used in the food, pharmaceutical and chemical industries
synthesis
O87172, -
cycloamylose will be used in the food, pharmaceutical and chemical industries
synthesis
-
production of cycloamylose; production of cycloamylose
synthesis
-
the recombinant enzyme is used to enzymatically-synthesized glycogen as a food ingredient
food industry
-
thermostable 4-alpha-glucanotransferase from Thermus scotoductus is used for rice cake production
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
nutrition
-
potential applications in the starch industry
synthesis
-
potential applications in the starch industry