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Information on EC 2.4.1.25 - 4-alpha-glucanotransferase
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EC Tree
2.4.1.25 4-alpha-glucanotransferaseIUBMB 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-alpha-1,6-glucosidase).
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Word Map
- 2.4.1.25
- starch
- maltose
- maltodextrins
- amylose
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transglycosylation
- glucans
- amylopectin
- cycloamylose
-
disproportionation
- malto-oligosaccharides
- maltotetraose
- maltohexaose
- alpha-glucans
- maltopentaose
- synthesis
- alpha-amylases
- amylo-1,6-glucosidase
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maltogenic
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malpq
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large-ring
- alpha-1,4-glucans
- biotechnology
- nutrition
- medicine
- analysis
- food industry
The enzyme appears in viruses and cellular organisms
Synonyms
amylomaltase, d-enzyme, 4-alpha-glucanotransferase, disproportionating enzyme, amase, maltosyltransferase, alphagt, alphagtase, mq-01, alpha-1,4-glucanotransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-alpha-glucanotransferase
4-alpha-GTase
4alphaGT
4alphaGTase
AMase
amylmaltase
amylomaltase
Cqm1
the ordered domain (residues 23-560) of surface receptor protein Cqm1 has amylomaltase activity
D-enzyme
debranching enzyme
debranching enzyme maltodextrin glycosyltransferase
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dextrin glycosyltransferase
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dextrin glycosyltransferase,
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dextrin transglycosylase
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disproportionating enzyme
DPE1
DPE2
EC 2.4.1.3
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formerly
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exo-MGTase
GDE
GH77
glycogen debranching enzyme
GTase
MalQ
maltodextrin glycosyltransferase
maltosyltransferase
MgtA
MmtA
MTase
oligo-1,4-1,4-glucantransferase
PyAMase
TAalphaGT
TLGT
TreX
additional information
amylomaltase
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D-enzyme
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disproportionating enzyme
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TreX
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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
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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
maltononaose + maltotriose = maltoundecaose + D-glucose
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)
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maltononaose + maltotriose = maltoundecaose + D-glucose
catalytic mechanism and domain structure and function
maltononaose + maltotriose = maltoundecaose + D-glucose
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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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-
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transglycosylation
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PATHWAY SOURCE
PATHWAYS
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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
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
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
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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
?
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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
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?
6-O-alpha-D-glucosyl-cyclodextrins + H2O
D-glucose + cyclodextrins
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?
6-O-alpha-D-glucosyl-cyclomalto-octaose + H2O
D-glucose + cyclodextrins
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?
64-O-alpha-maltooligosyl-pyridylamino-maltooctaose + maltohexaose
64-O-alpha-D-glucosyl-pyridylamino-maltooctaose + ?
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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
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?
amylopectin + D-glucose
small oligosaccharides
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without maltose
?
amylose
cycloamylose
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the enzyme produces a cycloamylose with a minimum degree of polymerization of 16
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?
barley starch + glycosyl acceptor
?
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transgenic barley amylose-only starch which consists of more than 99% amylose
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?
cassava starch + glycosyl acceptor
large ring-cyclodextrins 25-80
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?
cassava starch + glycosyl acceptor
large-ring cyclodextrins 24-29
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?
dodecyl-beta-maltoside + alpha-cyclodextrin
dodecyl-beta-maltooctaoside + ?
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?
dodecyl-beta-maltoside + starch
dodecyl-beta-maltooctaoside + ?
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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
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?
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)
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i.e. B5/84 + G6PA
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?
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
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?
maize starch + glycosyl acceptor
?
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100% amylopectin waxy maize starch
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?
maltodextrin + maltose
maltooligosaccharides + alpha-D-glucose
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?
maltoheptaose + glycosyl acceptor
maltose + D-glucose + maltooligosaccharides
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worst substrate
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?
maltoheptaose + maltotriose
maltononaose + D-glucose
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D-enzyme
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?
maltohexaose + maltodextrin
D-glucose + maltopentaose
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only amylomaltase, no polymers larger than the initial maltodextrin substrate, maltohexaose is a good donor substrate, but unable to function as an acceptor
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?
maltononaose + maltotriose
maltoundecaose + D-glucose
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D-enzyme
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?
maltooligosaccharides
maltooligosaccharides + D-glucose
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?
maltopentaose + maltotriose
homologous 1,4-alpha-D-glucans
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amylomaltose
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?
maltopentaose + maltotriose
maltoheptaose + D-glucose
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D-enzyme
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?
maltose + glycosyl acceptor
D-glucose
efficient transglycosylation activity
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?
maltosyl-alpha-(1->6)-puerarin
?
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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
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?
maltotetraose + maltotriose
glucose + maltoheptaose + maltodecaose
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D-enzyme
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?
maltotetraose + maltotriose
homologous 1,4-alpha-glucans
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amylomaltose
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?
maltotriose + glycosyl acceptor
D-glucose + maltose + maltotetraose + maltopentaose + maltohexaose
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?
maltotriose + maltotriose
D-glucose + maltopentaose + maltoheptaose + maltononaose + maltoundecaose
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D-enzyme
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?
maltotriose + maltotriose
glucose + maltooligosaccharides
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?
maltotriose + maltotriose
homologous alpha-1,4-D-glucans
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amylomaltose
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?