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Enzyme Nomenclature
Information on EC 2.4.1.25 - 4-alpha-glucanotransferase
Word Map on EC 2.4.1.25
- 2.4.1.25
- starch
- glucans
- maltodextrins
- mutans
- amylose
-
transglycosylation
- amylopectin
-
cycloamylose
-
disproportionation
-
water-insoluble
- malto-oligosaccharides
- synthesis
-
guanylyltransferase
- sobrinus
- acarbose
- maltohexaose
- maltotetraose
- maltopentaose
- alpha-glucans
- isoamylase
-
amylolytic
-
sucrose-dependent
-
alpha-1,4-glucans
- amylo-1,6-glucosidase
-
malpq
-
maltosyl
- litoralis
- alpha-amylases
- nutrition
- food industry
- biotechnology
- analysis
- medicine
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
2.4.1.25
-
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RECOMMENDED NAME
GeneOntology No.
4-alpha-glucanotransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
this entry covers the former separate entry for EC 2.4.1.3. (amylomaltase). The plant enzyme has been termed D-enzyme. An enzymic activity of this nature forms part of the mammalian and yeast glycogen debranching system (see EC 3.2.1.33 amylo-1,6-glucosidase)
-
-
-
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
reaction mechanism and catalytic cycle, the catalytic nucleophile changes conformation dramatically during the reaction, Gln256 on the 250s loop is involved in orienting the substrate in the +1 site. The absence of a suitable base in the covalent intermediate structure explains the low hydrolysis activity, overview
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
catalytic mechanism and domain structure and function
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strains CBS 513.88, NRRL3122, and N402, isozymes AgtA and AgtB encoded by genes agtA and agtB
-
-
alpha-1,4-glucanotransferase gene, GenBank accession no.; D-enzyme sequence
GenBank
-
-
-
ATCC 33923, nucleotide sequence accession number, deposited in DDBJ/EMBL/GenBank
SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
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
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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
-
-
-
-
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
?
-
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
-
-
?
6-O-alpha-D-glucosyl-cyclodextrins + H2O
D-glucose + cyclodextrins
-
-
-
?
6-O-alpha-D-glucosyl-cyclomalto-octaose + H2O
glucose + cyclodextrins
-
-
-
?
64-O-alpha-maltooligosyl-pyridylamino-maltooctaose + maltohexaose
64-O-alpha-D-glucosyl-pyridylamino-maltooctaose + ?
-
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
-
without maltose
?
amylose
cycloamylose
-
the enzyme produces a cycloamylose with a minimum degree of polymerization of 16
-
-
?
dodecyl-beta-maltoside + alpha-cyclodextrin
dodecyl-beta-maltooctaoside + ?
-
-
-
-
?
dodecyl-beta-maltoside + starch
dodecyl-beta-maltooctaoside + ?
-
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)
-
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
-
-
-
-
?
maltoheptaose + maltotriose
maltononaose + D-glucose
-
D-enzyme
-
?
maltohexaose + maltodextrin
D-glucose + maltopentaose
-
only amylomaltase, no polymers larger than the initial maltodextrin substrate, maltohexaose is a good donor substrate, but unable to function as an acceptor
-
?
maltononaose + maltotriose
maltoundecaose + D-glucose
-
D-enzyme
-
?
maltooligosaccharides
maltooligosaccharides + D-glucose
-
-
-
?
maltopentaose + maltotriose
homologous 1,4-alpha-D-glucans
-
amylomaltose
-
?
maltopentaose + maltotriose
maltoheptaose + D-glucose
-
D-enzyme
-
?
maltosyl-alpha-(1->6)-puerarin
?
-
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
-
?
maltotetraose + maltotriose
glucose + maltoheptaose + maltodecaose
-
D-enzyme
-
?
maltotetraose + maltotriose
homologous 1,4-alpha-glucans
-
amylomaltose
-
?
maltotriose + glycosyl acceptor
D-glucose + maltose + maltotetraose + maltopentaose + maltohexaose
-
-
-
?
maltotriose + maltotriose
D-glucose + maltopentaose + maltoheptaose + maltononaose + maltoundecaose
-
D-enzyme
-
?
maltotriose + maltotriose
glucose + maltooligosaccharides
-
-
-
?
maltotriose + maltotriose
homologous alpha-1,4-D-glucans
-
amylomaltose
-
?
starch + D-allose
oligosaccharides terminated by 4-O-alpha-D-glucopyranosyl-D-allose
-
-
-
?
starch + D-mannose
oligosaccharides terminated by 4-O-alpha-D-glucopyranosyl-D-mannose
-
-
-
?
starch + D-xylose
oligosaccharides terminated by 4-O-alpha-D-glucopyranosyl-D-xylose
-
-
-
?
starch + glycosyl acceptor
glucose + maltose + other oligosaccharides
-
-
-
?
starch + N-acetyl-D-glucosamine
oligosaccharides terminated by 4-O-alpha-D-glucopyranosyl-N-acetyl-D-glucosamine
-
-
-
?
tapioca starch + glycosyl acceptor
large-ring cyclodextrins
-
-
-
-
?
(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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
r
(alpha-1,4-D-glucan)m + H2O
(alpha-1,4-D-glucan)x + (alpha-1,4-D-glucan)m-x
-
-
-
r
(alpha-1,4-D-glucan)m + H2O
(alpha-1,4-D-glucan)x + (alpha-1,4-D-glucan)m-x
-
-
-
r
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharide
-
-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharide
-
maltose and a highly branched, soluble heteroglycan are excellent substrates for DPE2
-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
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
maltooligosaccharides
-
-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
-
-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
-
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
-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
-
-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
-
-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
-
-
-
?
6-O-alpha-D-glucosyl-cyclomaltoheptaose + H2O
D-glucose + cyclodextrins
-
-
-
-
-
6-O-alpha-D-glucosyl-cyclomaltoheptaose + H2O
D-glucose + cyclodextrins
-
-
-
?
amylose + D-glucose
low molecular mass oligosaccharides
-
-
?
amylose + D-glucose
low molecular mass oligosaccharides
-
synthetic amylose AS-320
-
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
-
-
cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
-
-
cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
-
-
cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
-
cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
-
cycloamylose
?
corn starch + glycosyl acceptor
large-ring cyclodextrins
-
-
-
-
?
corn starch + glycosyl acceptor
large-ring cyclodextrins
-
-
-
-
?
glutinous-rice starch + glycosyl acceptor
large-ring cyclodextrins
-
-
-
-
?
glutinous-rice starch + glycosyl acceptor
large-ring cyclodextrins
-
-
-
-
?
maltodextrin + maltose
maltooligosaccharides + H2O
-
catabolic processing of glycogen and maltodextrins
-
?
maltodextrin + maltose
maltooligosaccharides + H2O
-
catabolic processing of glycogen and maltodextrins
-
?
maltodextrin + maltose
maltooligosaccharides + H2O
-
catabolic processing of glycogen and maltodextrins
-
?
maltodextrin + maltose
maltooligosaccharides + H2O
-
catabolic processing of glycogen and maltodextrins
-
?
maltoheptaose + maltoheptaose
D-glucose + maltooligosaccharides
-
-
-
-
?
maltoheptaose + maltoheptaose
D-glucose + maltooligosaccharides
-
-
-
-
?
maltohexaose + maltohexaose
D-glucose + maltooligosaccharides
-
-
-
-
?
maltohexaose + maltohexaose
D-glucose + maltooligosaccharides
-
-
-
-
?
maltohexose + maltohexose
maltooligosaccharides
-
-
-
-
?
maltopentaose + maltopentaose
D-glucose + maltooligosaccharides
-
-
-
-
?
maltopentaose + maltopentaose
D-glucose + maltooligosaccharides
-
-
-
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
-
-
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
new oligosaccharides
-
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 + maltotriose
D-glucose + maltooligosaccharides
-
-
?
maltose + (1,4-alpha-glucan)n+1
D-glucose + (1,4-alpha-glucan)n+1
-
-
-
?
maltose + (1,4-alpha-glucan)n+1
D-glucose + (1,4-alpha-glucan)n+1
-
-
-
?
maltose + beta-cyclodextrin
6-O-alpha-maltosyl-beta-cyclodextrin
-
condensation reaction mechanism, overview
mass spectrometric product identification
-
?
maltose + beta-cyclodextrin
6-O-alpha-maltosyl-beta-cyclodextrin
-
condensation reaction mechanism, overview
mass spectrometric product identification
-
?
maltose + maltose
maltotriose + glucose
key role in maltose metabolism
-
-
?
maltotetraose + maltotetraose
D-glucose + maltooligosaccharides
-
-
-
-
?
maltotetraose + maltotetraose
D-glucose + maltooligosaccharides
-
-
-
-
?
maltotetraose + maltotetraose
maltooligosaccharides
-
-
-
-
?
maltotetraose + maltotriose
D-glucose + maltooligosaccharides
-
amylomaltose, most active with maltotetraose
-
?
maltotetraose + maltotriose
D-glucose + maltooligosaccharides
-
-
-
?
maltotetraose + maltotriose
D-glucose + maltooligosaccharides
-
-
?
maltotriose + maltodextrin
maltopentaose + ?
-
amylomaltase
-
?
maltotriose + maltodextrin
maltose + higher dextrins
-
-
-
?
maltotriose + maltotriose
D-glucose + maltooligosaccharides
-
-
-
?
maltotriose + maltotriose
D-glucose + maltooligosaccharides
-
-
-
?
maltotriose + maltotriose
maltooligosaccharides
-
most efficient substrate
-
-
?
maltotriose + maltotriose
maltooligosaccharides
-
most efficient substrate
-
-
?
maltotriose + maltotriose
maltopentaose + D-glucose
-
D-enzyme
-
?
maltotriose + maltotriose
maltopentaose + maltotetraose
-
-
-
?
pea starch + glycosyl acceptor
large-ring cyclodextrins
-
-
-
-
?
potato amylose + glycosyl acceptor
cycloamylose
-
-
the enzyme can produce cycloamyloses in the range 16–50 glucose residues
-
?
potato amylose + glycosyl acceptor
cycloamylose
-
-
the enzyme can produce cycloamyloses in the range 16 to more than 60 glucose residues
-
?
potato starch + maltose
large-ring cyclodextrins
-
-
-
-
?
rice starch + glycosyl acceptor
large-ring cyclodextrins
-
-
-
-
?
rice starch + glycosyl acceptor
large-ring cyclodextrins
-
-
-
-
?
starch + D-glucose
low molecular mass oligosaccharides
-
soluble starch
-
?
starch + maltopentaose
alpha-1,4-D-glucans
-
starch can serve as acceptor molecule in glycosyl transfer reactions
-
?
additional information
?
-
-
the smallest acceptor is glucose, the smallest donor is maltose
-
-
-
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
?
-
-
amylopectin is no substrate, maltose is not a product
-
-
-
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
?
-
-
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
?
-
-
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
?
-
-
glucose, maltose, maltotriose and maltotetraose are not acceptor molecules
-
-
-
additional information
?
-
-
does not use maltose, maltotriose or maltotetraose as acceptor substrates in maltodextrinyltransfer reactions
-
-
-
additional information
?
-
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
?
-
-
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
?
-
-
glucose, maltose and maltotriose can act as acceptor, only maltotriose can act as donor
-
-
-
additional information
?
-
-
glucose, maltose and maltotriose can act as acceptor, only maltotriose can act as donor
-
-
-
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 is inable to serve as a donor substrate, serving only as an acceptor substrate
-
-
-
additional information
?
-
-
D-galactose, sugar alcohols such as sorbitol and xylitol and glycerol are not effective as acceptors
-
-
-
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
?
-
-
maltose is inable to serve as a donor substrate, serving only as an acceptor substrate
-
-
-
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
?
-
-
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
?
-
-
D-galactose, sugar alcohols such as sorbitol and xylitol and glycerol are not effective as acceptors
-
-
-
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
?
-
-
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
?
-
-
D-galactose, sugar alcohols such as sorbitol and xylitol and glycerol are not effective as acceptors
-
-
-
additional information
?
-
-
does not act on 6-O-alpha-maltosyl cyclomaltoheptaose
-
-
-
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
?
-
-
glucose is the major product of the D-enzyme reaction
-
-
-
additional information
?
-
-
major pathway for starch degradation in chloroplasts
-
-
-
additional information
?
-
-
cannot use maltose or cyclohexaamylose as a substrate
-
-
-
additional information
?
-
-
D-enzyme, maltohexaose is no initial substrate
-
-
-
additional information
?
-
-
2 glycosyltransferases, amylomaltase and D-enzyme
-
-
-
additional information
?
-
-
D-enzyme, maltohexaose is no initial substrate
-
-
-
additional information
?
-
-
2 glycosyltransferases, amylomaltase and D-enzyme
-
-
-
additional information
?
-
-
acting on gelatinized food-grade potato starch, PyAMase produced a thermoreversible starch product with gelatin-like properties
-
-
-
additional information
?
-
-
acting on gelatinized food-grade potato starch, PyAMase produced a thermoreversible starch product with gelatin-like properties
-
-
-
additional information
?
-
-
appears to be exclusively oligo-1,4-1,4-glucantransferase-amylo 1,6-glucosidase and does not have isoamylase
-
-
-
additional information
?
-
-
does not act on 6-O-alpha-maltosyl cyclomaltoheptaose
-
-
-
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
?
-
-
glucose is the major product of the D-enzyme reaction
-
-
-
additional information
?
-
-
maltose is not a donor substrate, only weak acceptor activity
-
-
-
additional information
?
-
glucose is the major product of the D-enzyme reaction
-
-
-
additional information
?
-
-
D-glucosamine, N-acetyl-D-glucosamine and isomaltose have no activity as acceptors
-
-
-
additional information
?
-
-
glucose is the major product of the D-enzyme reaction
-
-
-
additional information
?
-
acts in concert with EC 2.4.1.1
-
-
-
additional information
?
-
-
the enzyme is involved in glycogen metabolism by selective cleavage of the outer side chain
-
-
-
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 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
?
-
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
?
-
-
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
?
-
-
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
-
-
-
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
?
-
-
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
?
-
-
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
?
-
-
glucose is the major product of the D-enzyme reaction
-
-
-
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
?
-
-
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
?
-
-
2 different 4-alpha-glucanotransferases, MTAse and Gtase
-
-
-
additional information
?
-
-
unable to use maltotriose as donor sugar or glucose as acceptor sugar
-
-
-
additional information
?
-
-
Gtase, glucose does not function as acceptor sugar, nor does it appear as reaction product
-
-
-
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
?
-
-
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
?
-
-
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
?
-
-
modification of granular corn starch with 4-alpha-glucanotransferase from Thermotoga maritima without induction of gelatinization, analysis of the morphology of the modified starches with light and scanning electron microscopy, the granule integrity is mostly maintained after enzyme treatment, although some granules are partially fragmented, amylose and amylopectin levels can be altered, solubility and paste clarity of themodified starches are much higher than those of raw starch, and it shows thermoreversibility between 4 and 75°C, X-ray diffraction and relative crystallinity, overview
-
-
-
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
?
-
-
amylomaltase from Thermus aquaticus catalyzes three types of transglycosylation reaction, as well as a weak hydrolytic reaction of alpha-1,4 glucan
-
-
-
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
?
-
-
modification of rice starch by the enzyme
-
-
-
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 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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
glucose can only be used as acceptor of maltosyl units
-
-
-
additional information
?
-
amylomaltases are capable of the synthesis of large cyclic glucans and the disproportionation of oligosaccharides
-
-
-
additional information
?
-
Thermus thermophilus AMase is among the most efficient 4-alpha-glucanotransferases in the alpha-amylase superfamily
-
-
-
additional information
?
-
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
?
-
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
?
-
-
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
?
-
-
glucose is the major product of the D-enzyme reaction
-
-
-
additional information
?
-
-
cannot use maltose or cyclohexaamylose as a substrate
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
Q8RXD9
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
maltooligosaccharides
-
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
-
-
?
maltodextrin + maltose
maltooligosaccharides + H2O
-
catabolic processing of glycogen and maltodextrins
-
?
maltodextrin + maltose
maltooligosaccharides + H2O
-
catabolic processing of glycogen and maltodextrins
-
?
maltodextrin + maltose
maltooligosaccharides + H2O
-
catabolic processing of glycogen and maltodextrins
-
?
maltodextrin + maltose
maltooligosaccharides + H2O
-
catabolic processing of glycogen and maltodextrins
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
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
?
-
-
the enzyme is involved in glycogen metabolism by selective cleavage of the outer side chain
-
-
-
additional information
?
-
-
the enzyme is involved in glycogen metabolism by selective cleavage of the outer side chain
-
-
-
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
?
-
O87172
Thermus thermophilus AMase is among the most efficient 4-alpha-glucanotransferases in the alpha-amylase superfamily
-
-
-
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
aplanin
-
Bay e 4609, pseudooligosaccharide resembling amylose with a hydroxymethylconduritol unit and a 4-amino-4-deoxy-D-chinorose residue linked to a varying number of alpha-D-glucose units from 7-30
acarbose
a strong mixed inhibitor with almost equal competitive and uncompetitive binding constants, acarbose is both bound in the active site and at another site
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cyclodextrin
-
the extent of 4-alpha-glucanotransferase activation increases with cyclodextrin concentration before reaching a constant value
-
maltoheptaose
-
stimulating effect of maltooligosaccharides on the conversion of amylose, 15 mM, relative activity 124%
maltohexaose
-
stimulating effect of maltooligosaccharides on the conversion of amylose, 15 mM, relative activity 144%
maltopentaose
-
stimulating effect of maltooligosaccharides on the conversion of amylose, 15 mM, relative activity 210%
maltose
-
stimulating effect of maltooligosaccharides on the conversion of amylose, relative activity 259%
maltotetraose
-
stimulating effect of maltooligosaccharides on the conversion of amylose, 15 mM, relative activity 246%
maltotriose
-
stimulating effect of maltooligosaccharides on the conversion of amylose, 15 mM, relative activity 210%
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kinetics of wild-type and mutant enzymes at pH 6.5 and 70°C, overview
-
additional information
additional information
initial rate kintics
-
additional information
additional information
-
at 25 mM alpha-cyclodextrin, the reaction rate decreases with increasing dodecyl-beta-maltoside concentration, and when the alpha-cyclodextrin concentration is varied at fixed dodecyl-beta-maltoside concentration, an S shaped curve is obtained
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00048
maltotriose
Thermus brockianus
Q2VJA0
mutant Q256G, pH 6.0, 70°C; mutant W258G, pH 6.0, 70°C
188
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0556
beta-cyclodextrin
-
pH 5.5, 75°C, recombinant His-tagged enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
5.5
6 - 8
6.5
6.7
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 7.5
pH dependence of wild-type and mutant enzymes, D293N and E340Q are active below pH 6.5 and pH 5.5, respectively, but precipitate during the necessary prolonged incubation times, wild-type Tt AMase precipitates below pH 5.5 under similar extended incubation times as well, overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
45
70
75
80
90
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60 - 100
-
60°C: about 50% of maximal activity, 100°C: about 30% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.1
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the enzyme is present in the amyloplast of developing endosperm
-
enzyme is more active in longissimus dorsi than in masseter. In both muscles the activity begins to fall at temperatures below 39°C and is almost zero when the temperature decreases to below 15°C. The activity of GDE may control the rate of glycogenolysis and glycolysis, but does not block rapid glycolysis and pH decrease when the temperature is high
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)
Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)
Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
56000
57220
62000
64950
estimated from amino acid sequence, deduced from nucleotide sequence
71000
74000
81000
174900
-
estimated from amino acid sequence, deduced from nucleotide sequence
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer or tetramer
homodimer
monomer
tetramer
additional information
dimer
-
1 * 38000 + 1 * 47000, amylomaltase; 1 * 52000 + 1 * 63000, D-enzyme
dimer
-
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
-
at pH 7.0, gel filtration and analytical sedimentation ultracentrifugation
-
dimer or tetramer
-
at pH 5.5, gel filtration and analytical sedimentation ultracentrifugation
dimer or tetramer
the enzyme exists in two oligomeric states in solution, as a dimer and tetramer
dimer or tetramer
-
at pH 5.5, gel filtration and analytical sedimentation ultracentrifugation
-
tetramer
-
at pH 5.5-6.5 in presence of DMSO, gel filtration and analytical sedimentation ultracentrifugation
tetramer
-
at pH 5.5-6.5 in presence of DMSO, gel filtration and analytical sedimentation ultracentrifugation
-
additional information
-
DPE2 is a modular protein consisting of a family 77 glycosyl hydrolase domain, similar to DPE1, but unlike DPE1 the domain is interrupted by an insertion of about 150 amino acids as well as an N-terminal extension that consists of two carbohydrate binding modules, domain structure and functiosn, overview
additional information
-
the tetramer shows a 4fold higher catalytic activity than the dimer
additional information
the structural lid, amino acids 99-97, at the active site generated by the tetramerization is closely associated with the bifunctionality and in particular with the alpha-1,4-transferase activity
additional information
-
the structural lid, amino acids 99-97, at the active site generated by the tetramerization is closely associated with the bifunctionality and in particular with the alpha-1,4-transferase activity
additional information
-
the tetramer shows a 4fold higher catalytic activity than the dimer
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycolipoprotein
-
the enzyme is cell wall-associated via glycosylphosphatidylinositol anchoring
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 0.1 M bis-Tris pH 5.5 and 2.0 M ammonium sulfate
-
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 18°C, dimeric crystal from 16% PEG 8000, 0.2 M NaCl, and 0.1 M CHES buffer, pH 9.5, tetrameric crystal form from 2.2 M ammonium phosphate and 0.1 M Tris-HCl buffer, pH 8.5. For the acarbose intermediate complex crystal, 0.1% acarbose is added to the protein, followed by incubation for 1 h prior to the setup of the crystal in 8% PEG 3000, 0.2M lithium sulfate, and 0.1 M imidazole buffer, pH 8.0, cyroprotection by 20% glycerol in mother liquor, in both crystal forms, the asymmetric unit consists of one dimer, X-ray diffraction structure determination and analysis at 2.8-3.0 A resolution
crystallized in 2 forms, I and II, form I crystals belongs to hexagonal space group P6(4)22, form II crystals to orthorhombic space group P2(1)2(1)2; hanging drop vapor diffusion method at 25°C, crystal structure of the enzyme with and without an inhibitor, acarbose. The acarbose-bound structure clarifies that Glu123 and Asp214 are the catalytic nucleophile and acid/base catalyst, respectively
-
Gtase, hanging drop method, inhibitor complex,crystals belong to space group I222, unit-cell dimensions a = 92.6 A, b = 180.3 A, c = 199.2 A, free Gtase crystals a = 94.5 A, b = 181.4 A, c = 197.3 A
-
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
purified recombinant enzyme, hanging drop vapour diffusion method, 0.003 ml of protein solution containing 10 mM MES-NaOH, pH 6.5, with 1 mM dithiothreitol is mixed with 0.001-0.003 ml of reservoir solution containing 0.4-0.8 M sodium malonate, pH 5.6, and 1 mM dithiothreitol, equilibration against reservoir solution at room temperature, 1 week, for enzyme-acarbose complexing the crystals are soaked in 0.5 ml of 0.8 M sodium malonate, pH 5.6, with 5 mg/ml acarbose and with or without and 4-deoxyglucose, for 30 min, X-ray diffraction structure determination and analysis at 1.9-2.5 A resolution
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9
-
the recombinant enzyme maintains more than 80% of its activity at a temperature range of 50-80°C and a pH range of 5.0-9.0
704054
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35 - 40
-
at short incubation time for 15 min at 40°C, the remaining activity of the wild type enzyme is 39.5%, whereas for 30 min incubation, the activity remained is 15.2%. At 35°C for a longer incubation time of 3 h, the remaining activity of the wild type enzyme is 45%
37 - 42
-
D-enzyme, activity decreases rapidly above 37°C and is almost completely lost at 42°C
37 - 80
-
stable at 37°C, retains more than 90% of its maximum activity between 55-80°C, half-life of activity of about 3 h at 80°C
50
50 - 80
-
the recombinant enzyme maintains more than 80% of its activity at a temperature range of 50-80°C and a pH range of 5.0-9.0
80
85
90
100
85
stable up to, retains 50% activity after incubation at 80°C for 24 h, loses all activity after incubation at 100°C for 10 min
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable to freezing, glycerol reduces activity and cannot be used to stabilize the enzyme at freezing temperatures
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stored in purification buffer, activity is stable for over 6 months
-
-80°C, purified recombinant enzyme, 20 mM sodium phosphate buffer containing 15% glycerol, pH 7.0, no decrease in acivity observed for 1 month
-
4°C, purified enzyme in buffer shows little or no loss of activity in 1 month
-
4°C, relatively stable at low temperatures, may be stored for many months in a cold room with relatively little loss of activity
-
4°C, stable in 20 mM bis-Tris-propane buffer, pH 6.5, containing 10% glycerol, no loss of activity over 6 months
-
4°C, stored as a suspension in 3.2 M ammonium sulfate, no significant loss of activity for at least 1 month
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
iminodiacetic acid-Sepharose column chromatography and Superdex 200 gel filtration
native and recombinant enzyme
Ni HiTrap column chromatography and Superdex 75 gel filtration
partial
recombinant enzyme
recombinant His-tagged alpaGTase 2.9fold from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by heat treatment and nickel affinity chromatography, removal of the His-tag through cleavage with bovine thrombin
recombinant His-tagged enzyme from Escherichia coli strain MC1061 by nickel affinity chromatography
-
recombinant His-tagged TsalphaGT from Escherichia coli strain MC1061 by nickel affinity chromatography to homogeneity
-
recombinant His6-tagged MalQ from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
recombinant wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; STA11, both cDNA and gDNA corresponding to the D-enzyme cloned
chromosomal gene cloned and expressed in Escherichia coli and Corynebacterium glutamicum
-
cloned into pTrc99A plasmid vector and expressed in Escherichia coli JM105
-
expressed in Escherichia coli BL21 Star (DE3) One Shot cells
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
expression of wild-type and mutant enzymes in Escherichia coli, sequence comparison
gene malQ, DNA and amino acid sequence determination and analysis, phylogenetic tree, sequence comparisons, expression of the His6-tagged enzyme in Escherichia coli strain BL21 (DE3)
gene treX, cloning from the trehalose biosynthesis gene cluster, expression of the His-tagged enzyme in Escherichia coli
-
genes agtA and agtB, DNA and amino acid sequence determination and analysis, phylogenetic tree, overexpression in Aspergillus niger strain MGG029, subcloning in Escherichia coli
-
genes for amylomaltase are part of the glycogen operon
genes of wild-type and mutant enzymes are coexpressed in Escherichia coli cells with GroELS, tRNA(AGA), and tRNA(AGG)
-
human glycogen debrancher gene assigned to chromosome 1p21, cloned and expressed in insect cells
-
putative gene identified in the genome
expressed in Escherichia coli BL21(DE3) cells
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A406L
-
the mutant shows higher thermostability at 35-40°C, higher intermolecular transglucosylation activity with an upward shift in the optimum temperature and a slight increase in the optimum pH for disproportionation and cyclization reactions compared to the wild type enzyme. The mutant shows higher specific activities for starch transglucosylation (2.1fold) and disproportionation (1.4fold) than those of the wild type
A406V
-
the mutant shows higher thermostability at 50°C, higher intermolecular transglucosylation activity with an upward shift in the optimum temperature and a slight increase in the optimum pH for disproportionation and cyclization reactions compared to the wild type enzyme. The mutant shows higher specific activities for starch transglucosylation (2.8fold) and disproportionation (2.1fold) than those of the wild type
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
A406L
-
the mutant shows higher thermostability at 35-40°C, higher intermolecular transglucosylation activity with an upward shift in the optimum temperature and a slight increase in the optimum pH for disproportionation and cyclization reactions compared to the wild type enzyme. The mutant shows higher specific activities for starch transglucosylation (2.1fold) and disproportionation (1.4fold) than those of the wild type
-
A406V
-
the mutant shows higher thermostability at 50°C, higher intermolecular transglucosylation activity with an upward shift in the optimum temperature and a slight increase in the optimum pH for disproportionation and cyclization reactions compared to the wild type enzyme. The mutant shows higher specific activities for starch transglucosylation (2.8fold) and disproportionation (2.1fold) than those of the wild type
-
W229H
-
kcat/KM value of transglycosylation activity significantly decreases to about 15% of wild-type, kcat/Km value of hydrolysis activity changes little
D214N
-
the specific activity of the D214N mutant is decreased about 10000fold as compared with that of the wild-type enzyme
E123Q
-
the specific activity of the mutant enzyme toward maltotriose is about 15000fold lower than the specific activity of the wild-type enzyme
E129Q
-
the specific activity of the mutant enzyme is almost the same as that of the wild-type enzyme
D214N
-
the specific activity of the D214N mutant is decreased about 10000fold as compared with that of the wild-type enzyme
-
Y54A
Y54C
Y54D
Y54E
Y54F
Y54G
Y54H
Y54I
Y54K
Y54L
Y54M
Y54N
Y54P
Y54Q
Y54R
Y54S
Y54T
Y54V
Y54W
F251G
mutation results in significantly lower glucose production but increased maltose production from maltopentose substrates, showing an altered substrate-binding affinity
Q256G
mutation results in increased Km for maltotriose and a sharp decrease of the transglycosylation factor for maltose
W258G
mutant shows neither cyclization nor coupling activity, suggesting that residue Trp258 plays an essential role in all catalytic activities including hydrolysis and transglycosylation activities
D293A
site-directed mutagenesis of the active site nucleophile, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
D293N
site-directed mutagenesis of the active site nucleophile, the D293N mutation reduces the pH stability of the enzyme, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
D294S
site-directed mutagenesis, the mutant shows highly reduced kcat and reduced activity with malto-oligomers compared to the wild-type enzyme
D395A
site-directed mutagenesis of the active site transition stabilizer, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
D395N
site-directed mutagenesis of the active site transition stabilizer, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
E340A
site-directed mutagenesis of the active site general acid/base catalyst, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
E340Q
site-directed mutagenesis of the active site general acid/base catalyst, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
E758Q
the mutant shows highly reduced activity compared to the wild-type enzyme
F366L
site-directed mutagenesis, the mutant shows reduced kcat compared and reduced activity with malto-oligomers compared to the wild-type enzyme
additional information
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
Y54W
-
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
additional information
-
the glycosyl hydrolase domain alone provides disproportionating activity with a much higher affinity for short maltodextrins than the complete wild-type enzyme, while absence of the carbohydrate binding modules completely abolishes activity with large complex carbohydrates, reflecting the presumed function of DPE2 in vivo
additional information
-
an agtA knockout of Aspergillus niger shows an increased susceptibility towards the cell wall-disrupting compound, phenotypic characterization of CFW hypersensitive DELTAagtA strain and AgtA/AgtB overexpression strains, overview
additional information
mutations in the N-terminal region result in a sharp increase in alpha-1,4-transferase activity and a reduced level of alpha-1,6-glucosidase activity, overview
additional information
-
mutations in the N-terminal region result in a sharp increase in alpha-1,4-transferase activity and a reduced level of alpha-1,6-glucosidase activity, overview
additional information
-
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 100000–1000000) 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
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 100000–1000000) and produces cyclo-amyloses with DP of 19 through 35 from amylose molecules
-
additional information
-
enzymatic modification of rice starch to produce highly branched amylopectin and amylose using alpha-glucanotransferase and maltogenic amylase, overview
additional information
the deletion mutant DELTAN130 is unable to use glycogen but has high disproportionating activity with maltodextrins
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
investigation of molecular characteristics, microstructures, and physicochemical properties of modified starch gels prepared from partial enzyme treatments of the corn and rice starch pastes. Unlike the native and partially modified normal starches, the native and partially modified waxy starches can not form gels strong enough for textural analysis after 24 h for gel setting. The partially modified normal starches show specific apparent amylose contents and maximum iodine absorption wavelength, as well as the tri-modal molecular weight profiles and flatter side-chain distributions. The partially modified normal starch gels possess fractured surfaces with discontinuous crystalline fibrous assembly, which result in more brittle, rigid, and resilient gels compared with the native gels
biotechnology
-
industrial production of cycloamylase with mutant enzyme Y54G, which shows high cyclization activity and low hydrolytic activity
food industry
medicine
nutrition
synthesis
food industry
-
thermostable 4-alpha-glucanotransferase from Thermus scotoductus is used for rice cake production
food industry
-
TmalphaGT can be used to produce granular corn starch, which contains amylose and amylopectin having lower molecular weights and a thermoreversible gelation property
food industry
-
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
cycloamylose will be used in the food, pharmaceutical and chemical industries
nutrition
-
acting on gelatinized food-grade potato starch, PyAMase produced a thermoreversible starch product with gelatin-like properties. This thermoreversible gel has potential applications in the food industry
nutrition
-
acting on gelatinized food-grade potato starch, PyAMase produced a thermoreversible starch product with gelatin-like properties. This thermoreversible gel has potential applications in the food industry
-
synthesis
cycloamylose will be used in the food, pharmaceutical and chemical industries
synthesis
-
the enzyme is useful in the enzymatic synthesis of dimaltosyl-beta-cyclodextrin via a transglycosylation reaction
synthesis
-
the recombinant enzyme is used to enzymatically-synthesized glycogen as a food ingredient
synthesis
-
combination of maltogenic amylase reactions from Bacillus stearothermophilus and 4-alpha-glucanotransferase from Thermus scotoductus to increase the water solubility of puerarin, an isoflavonoid derived from Radix puerariae. The puerarin transfer products, including maltosyl-alpha-(1->6)-puerarin as a major product, are reacted with alpha-glucanotransferase in the presence of amylose. The maltosyl-alpha-(1->6)-puerarin-cycloamylose complex is formed by an elongation reaction and cyclization by alpha-glucanotransferase. The encapsulation of puerarin or glycosylated puerarin with a macrocyclic amylose is widely applicable both to improving the water solubility of the compound and stabilizing it during cold storage
synthesis
-
development of an efficient biocatalytic production process of cycloamyloses directly from sucrose by use of Synechocystis sp. 4-alpha-glucanotransferase and Neisseria polysaccharea amylosucrase. From one-pot synthesis, the maximum cycloamylose yield of 9.6%, w/w with 0.3 M sucrose is achieved with 10 units/ml of amylosucrase and 0.1 unit/ml of 4-alpha-glucanotransferase at 40°C for a 3 h reaction in a simultaneous dual enzyme reaction mode. The size of linear alpha-(1,4)-glucan is positively related to the cycloamylose productivity by 4-alpha-glucanotransferase in a hyperbolic manner. The dual enzyme reaction converts sucrose directly to cycloamyloses via in situ transient linear alpha-(1,4)-glucan as an soluble intermediate
synthesis
-
the enzyme is useful in the enzymatic synthesis of dimaltosyl-beta-cyclodextrin via a transglycosylation reaction
-
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