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 hide
2.4.1.25
-
RECOMMENDED NAME
GeneOntology No.
4-alpha-glucanotransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
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
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
glycogen degradation I
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-
glycogen degradation II
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-
glycogen metabolism
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-
Metabolic pathways
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-
Starch and sucrose metabolism
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-
starch degradation
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-
starch degradation II
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starch degradation V
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sucrose biosynthesis II
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-
SYSTEMATIC NAME
IUBMB Comments
(1->4)-alpha-D-glucan:(1->4)-alpha-D-glucan 4-alpha-D-glycosyltransferase
This entry covers the former separate entry for EC 2.4.1.3 (amylomaltase). The plant enzyme has been termed D-enzyme. An enzymic activity of this nature forms part of the mammalian and yeast glycogen debranching system (see EC 3.2.1.33 amylo-alpha-1,6-glucosidase).
CAS REGISTRY NUMBER
COMMENTARY hide
9032-09-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strains CBS 513.88, NRRL3122, and N402, isozymes AgtA and AgtB encoded by genes agtA and agtB
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
Borrelia burgdorferi
bovine
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
strain 137C
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-
Manually annotated by BRENDA team
NCIMB 7423
-
-
Manually annotated by BRENDA team
carrot
-
-
Manually annotated by BRENDA team
strain ML 30
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-
Manually annotated by BRENDA team
Ml 308
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-
Manually annotated by BRENDA team
chicken
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-
Manually annotated by BRENDA team
human
-
-
Manually annotated by BRENDA team
barley
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-
Manually annotated by BRENDA team
sweet potato
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
NRRL B3389
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Manually annotated by BRENDA team
NRRL B3389
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-
Manually annotated by BRENDA team
IM2
-
-
Manually annotated by BRENDA team
KOD1
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-
Manually annotated by BRENDA team
KOD1
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
tomato
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Manually annotated by BRENDA team
spinach
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-
Manually annotated by BRENDA team
dogfish
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-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
strain P2, gene treX
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Manually annotated by BRENDA team
strain YT-1
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Manually annotated by BRENDA team
broad bean, L.major
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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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
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
(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
(alpha-1,4-D-glucan)m + H2O
(alpha-1,4-D-glucan)x + (alpha-1,4-D-glucan)m-x
show the reaction diagram
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharide
show the reaction diagram
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
show the reaction diagram
1,4-alpha-D-glucan + glucose
maltooligosaccharides
show the reaction diagram
2-chloro-4-nitrophenyl 4''',6''''-O-(3-oxobutylidene)maltopentaoside + D-glucose
?
show the reaction diagram
-
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
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
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
-
without maltose
?
amylopectin + maltopentaose
maltooligosaccharides
show the reaction diagram
amylopectin + maltose
?
show the reaction diagram
-
Gtase
-
-
?
amylose
?
show the reaction diagram
amylose
cycloamylose
show the reaction diagram
-
the enzyme produces a cycloamylose with a minimum degree of polymerization of 16
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-
?
amylose + ?
cycloamylose + ?
show the reaction diagram
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-
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-
?
amylose + D-glucose
low molecular mass oligosaccharides
show the reaction diagram
amylose + maltopentaose
cyclic alpha-1,4-glucan
show the reaction diagram
amylose + maltopentaose
maltooligosaccharides
show the reaction diagram
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
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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)
show the reaction diagram
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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
show the reaction diagram
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-
-
-
?
glycogen + maltooligosaccharides
D-glucose + ?
show the reaction diagram
-
-
-
?
linear maltooligosaccharides + starch
?
show the reaction diagram
maltodextrin + D-glucose
maltooligosaccharides
show the reaction diagram
-
-
-
?
maltodextrin + maltodextrin
maltooligosaccharides
show the reaction diagram
maltodextrin + maltose
maltooligosaccharides + H2O
show the reaction diagram
maltoheptaose + maltoheptaose
?
show the reaction diagram
-
-
-
?
maltoheptaose + maltoheptaose
D-glucose + maltooligosaccharides
show the reaction diagram
maltoheptaose + maltoheptaose
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
?
show the reaction diagram
-
-
-
?
maltohexaose + maltohexaose
D-glucose + maltooligosaccharides
show the reaction diagram
maltohexaose + maltohexaose
maltooligosaccharides
show the reaction diagram
-
-
-
-
?
maltohexaose + maltopentaose
maltooligosaccharides
show the reaction diagram
maltohexaose + maltotriose
D-glucose + maltooligosaccharides
show the reaction diagram
-
-
-
?
maltohexaose + maltotriose
maltodextrins
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
maltopentaose + maltodextrin
maltose + higher dextrins
show the reaction diagram
-
-
-
?
maltopentaose + maltopentaose
?
show the reaction diagram
-
-
-
?
maltopentaose + maltopentaose
D-glucose + maltooligosaccharides
show the reaction diagram
maltopentaose + maltopentaose
maltooligosaccharides
show the reaction diagram
maltopentaose + maltopentaose
new oligosaccharides
show the reaction diagram
maltopentaose + maltotriose
D-glucose + maltooligosaccharides
show the reaction diagram
maltopentaose + maltotriose
homologous 1,4-alpha-D-glucans
show the reaction diagram
-
amylomaltose
-
?
maltopentaose + maltotriose
maltodextrins
show the reaction diagram
maltopentaose + maltotriose
maltoheptaose + D-glucose
show the reaction diagram
-
D-enzyme
-
?
maltose + (1,4-alpha-glucan)n+1
D-glucose + (1,4-alpha-glucan)n+1
show the reaction diagram
maltose + beta-cyclodextrin
6-O-alpha-maltosyl-beta-cyclodextrin
show the reaction diagram
maltose + maltose
maltooligosaccharides
show the reaction diagram
-
-
-
-
?
maltose + maltose
maltotriose + glucose
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
maltotetraitol
maltopentaitol + ?
show the reaction diagram
maltotetraose + maltodextrin
maltose + higher dextrins
show the reaction diagram
-
-
-
?
maltotetraose + maltopentaose
maltooligosaccharides
show the reaction diagram
maltotetraose + maltotetraose
?
show the reaction diagram
-
-
-
?
maltotetraose + maltotetraose
D-glucose + maltooligosaccharides
show the reaction diagram
maltotetraose + maltotetraose
maltooligosaccharides
show the reaction diagram
-
-
-
-
?
maltotetraose + maltotriose
D-glucose + maltooligosaccharides
show the reaction diagram
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
maltotheptaose + maltotriose
D-glucose + maltooligosaccharides
show the reaction diagram
-
-
-
?
maltotheptaose + maltotriose
maltodextrins
show the reaction diagram
maltotriose
maltooligosaccharides
show the reaction diagram
maltotriose + acceptor
glucose + maltose + maltotetraose + maltopentaose + maltohexaose
show the reaction diagram
-
-
-
?
maltotriose + amylopectin
?
show the reaction diagram
-
-
-
-
?
maltotriose + maltodextrin
maltopentaose + ?
show the reaction diagram
maltotriose + maltodextrin
maltose + higher dextrins
show the reaction diagram
maltotriose + maltotriose
?
show the reaction diagram
-
-
-
-
-
maltotriose + maltotriose
D-glucose + maltooligosaccharides
show the reaction diagram
maltotriose + maltotriose
D-glucose + maltopentaose
show the reaction diagram
-
-
-
-
?
maltotriose + maltotriose
D-glucose + maltopentaose + maltoheptaose + maltononaose + maltoundecaose
show the reaction diagram
-
D-enzyme
-
?
maltotriose + maltotriose
glucose + maltooligosaccharides
show the reaction diagram
-
-
-
?
maltotriose + maltotriose
homologous alpha-1,4-D-glucans
show the reaction diagram
-
amylomaltose
-
?
maltotriose + maltotriose
maltodextrins
show the reaction diagram
maltotriose + maltotriose
maltooligosaccharides
show the reaction diagram
-
-
-
-
?
maltotriose + maltotriose
maltopentaose + D-glucose
show the reaction diagram
maltotriose + maltotriose
maltopentaose + maltotetraose
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
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
starch + D-glucose
oligosaccharides
show the reaction diagram
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 + glucose
maltotriose + ?
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
starch + maltose
?
show the reaction diagram
-
Gtase
-
-
?
starch + methyl-alpha-D-glucoside
?
show the reaction diagram
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
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
show the reaction diagram
maltodextrin + maltose
maltooligosaccharides + H2O
show the reaction diagram
maltopentaose + maltopentaose
maltooligosaccharides
show the reaction diagram
additional information
?
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
D-enzyme, slight inhibition
acarbose
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
phenyl-beta-D-glucoside
-
competitive inhibition
Tris
-
D-enzyme, 50 mM, 35% inhibition
Zn2+
-
D-enzyme
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10.5 - 11.2
6-O-alpha-D-glucosyl-cyclomaltoheptaose
18
dodecyl-beta-maltoside
-
pH 5.2, 60C, 300 mM alpha-cyclodextrin
1.5 - 5.7
maltoheptaose
3.2 - 4.5
maltohexaose
4.2 - 6.9
maltopentaose
8.3 - 71
maltose
1.591
maltosyl-beta-cyclodextrin
-
pH 5.5, 75C
2.1 - 7.1
maltotetraose
2 - 165
maltotriose
2.8 - 3
phi-dextrin
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.99 - 213
maltoheptaose
3.26 - 304
maltohexaose
3.98 - 329
maltopentaose
1.3
maltose
Aquifex aeolicus
-
pH 6.6, 70C
0.0113
maltosyl-beta-cyclodextrin
Sulfolobus solfataricus
-
pH 5.5, 75C
0.97 - 425
maltotetraose
0.0017 - 317
maltotriose
additional information
additional information
Pyrococcus furiosus
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00035 - 0.0078
maltotriose
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003 - 0.004
acarbose
0.0556
beta-cyclodextrin
-
pH 5.5, 75C, recombinant His-tagged enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0027
mutant E758Q
1.36
-
-
5.19
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
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
recombinant enzyme
7.5 - 8
-
-
7.6 - 7.7
-
both amylomaltase and D-enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 6
-
-
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
recombinant enzyme
70 - 75
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 55
-
-
60 - 100
-
60C: about 50% of maximal activity, 100C: about 30% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
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the enzyme is present in the amyloplast of developing endosperm
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Aquifex aeolicus (strain VF5)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
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)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51900
-
SDS-PAGE
53000
-
SDS-PAGE
54000
-
gel filtration
59500
native enzyme, SDS-PAGE
64950
estimated from amino acid sequence, deduced from nucleotide sequence
65000
precursor, SDS-PAGE
70000 - 80000
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sedimentation equilibrium
76690
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calculated from cDNA
77880
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calculated from cDNA
79000
-
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
168000
-
gel filtration
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
COMMENTARY hide
LITERATURE
dimer or tetramer
homodimer
monomer
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycolipoprotein
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the enzyme is cell wall-associated via glycosylphosphatidylinositol anchoring
Crystallization/COMMENTARY
ORGANISM
UNIPROT
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
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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
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 25C, 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
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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
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crystals belong to space group P6(4) with cell parameters a = b = 154 A and c = 64 A
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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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 11
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stable
662665
3 - 8
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loses 40% of the activity at pH 3.0, 80% at pH 8.0
488995
4
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no activity detected
489000
4 - 10
-
489016
4 - 7.5
pH stability of wild-type and mutant enzy