3.2.1.20: alpha-glucosidase
This is an abbreviated version!
For detailed information about alpha-glucosidase, go to the full flat file.
Word Map on EC 3.2.1.20
-
3.2.1.20
-
lactase
-
acarbose
-
maltose
-
lysosomal
-
disaccharidase
-
postprandial
-
mellitus
-
border
-
brush
-
pompe
-
glycogen
-
starch
-
alpha-amylase
-
mucosal
-
aminopeptidase
-
hyperglycemia
-
antidiabetic
-
jejunal
-
amylase
-
beta-glucosidase
-
sulfonylurea
-
meal
-
trehalase
-
ileum
-
glucoamylase
-
glycemic
-
metformin
-
villus
-
glycosidases
-
thiazolidinediones
-
alpha-mannosidase
-
hypoglycemic
-
biguanides
-
brush-border
-
glycogenosis
-
sulphonylureas
-
alpha-galactosidase
-
maltotriose
-
non-insulin-dependent
-
peptidase-4
-
1-deoxynojirimycin
-
n-acetyl-beta-glucosaminidase
-
carbohydrases
-
antihyperglycemic
-
castanospermine
-
infantile-onset
-
alpha-fucosidase
-
cellobiase
-
medicine
-
repaglinide
-
flatulence
-
synthesis
-
agriculture
-
biotechnology
-
nutrition
-
diagnostics
- 3.2.1.20
- lactase
- acarbose
- maltose
- lysosomal
- disaccharidase
-
postprandial
- mellitus
- border
-
brush
- pompe
- glycogen
- starch
- alpha-amylase
- mucosal
- aminopeptidase
- hyperglycemia
-
antidiabetic
- jejunal
- amylase
- beta-glucosidase
- sulfonylurea
- meal
- trehalase
- ileum
- glucoamylase
-
glycemic
- metformin
- villus
- glycosidases
- thiazolidinediones
- alpha-mannosidase
-
hypoglycemic
- biguanides
-
brush-border
- glycogenosis
-
sulphonylureas
- alpha-galactosidase
- maltotriose
-
non-insulin-dependent
-
peptidase-4
- 1-deoxynojirimycin
- n-acetyl-beta-glucosaminidase
-
carbohydrases
-
antihyperglycemic
- castanospermine
-
infantile-onset
- alpha-fucosidase
- cellobiase
- medicine
- repaglinide
-
flatulence
- synthesis
- agriculture
- biotechnology
- nutrition
- diagnostics
Reaction
Synonyms
6-phospho-alpha-glucosidase, AAGR-1, AAGR-2, AAGR-3, AAGR-4, acid alpha-glucosidase, acid alpha-glucoside hydrolase, acid GAA, acid maltase, acidic alpha-glucosidase, AG, AgdB, AGL, AglA, aGlu, alglucosidase alfa, alpha-1,4-glucosidase, alpha-D-glucosidase, alpha-D-glucoside glucohydrolase, alpha-GD, alpha-glucopyranosidase, alpha-glucosid-specific GH4 enzyme, alpha-glucosidase, alpha-glucosidase B, alpha-glucosidase I, alpha-glucosidase II, alpha-glucosidase III, alpha-glucosidase MAL12, alpha-glucosidase MAL32, alpha-glucosidase type I, alpha-glucosidase type IV, alpha-glucoside glucohydrolase, alpha-glucoside hydrolase, alpha-transglucosidase, alphaGlu1, alphaGlu2, alphaGlu3, alphaGluFa, Amy112, CHEI, CWH41, exo-alpha-l, 4-glucosidase, exo-alpha-l,4-glucosidase, GAA, GH13 alpha-glucosidase, GluA, glucoamylase, glucoinvertase, glucosidoinvertase, glucosidosucrase, GlyFa1, GlyFa2, GSJ, HBG III, HBGase I, HBGase II, HBGase III, high pI alpha-glucosidase, intestinal alpha-glucosidase, intestinal maltase, JHGase I, MAL12, MAL2, MAL32, MalA, MalH, maltase, maltase glucoamylase, maltase-glucoamylase, maltodextrin glucosidase, MalZ, MGAM, More, myozyme, NAG, neutral alpha-glucosidase, PalH, Pars_2044, phospho-alpha-glucosidase, R-glucosidase, recombinant human GAA, rhGAA, Saci1160, st2525, Ta0298, TcaAG, TtGluA
ECTree
3.2.1.20 alpha-glucosidaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.2.1.20 - alpha-glucosidase
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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
1-O-alpha-D-glucopyranosyl-beta-D-fructofuranoside + H2O
alpha-D-glucose + D-fructose
-
-
-
?
3-O-alpha-D-glucopyranosyl-D-fructose + H2O
alpha-D-glucose + D-fructose
-
-
-
?
4-methylumbelliferyl alpha-D-galactopyranoside + H2O
4-methylumbelliferone + alpha-D-galactopyranose
-
-
-
?
4-methylumbelliferyl alpha-D-glucopyranoside + H2O
4-methylumbelliferol + alpha-D-glucopyranose
4-methylumbelliferyl alpha-D-glucopyranoside + H2O
4-methylumbelliferone + alpha-D-glucopyranose
4-methylumbelliferyl alpha-D-glucopyranoside + H2O
4-methylumbelliferone + alpha-D-glucose
-
assay at pH 4.0 or 6.5, 37°C
-
-
?
4-methylumbelliferyl alpha-D-glucoside + H2O
4-methylumbelliferol + alpha-D-glucose
-
synthetic fluorogenic substrate, competitive to the other substrates
-
-
?
4-methylumbelliferyl alpha-D-glucoside + H2O
4-methylumbelliferone + alpha-D-glucose
-
-
-
?
4-methylumbelliferyl-alpha-D-glucopyranoside + H2O
4-methylumbelliferone + alpha-D-glucose
4-nitrophenyl 2-deoxy-alpha-D-glucopyranoside + H2O
4-nitrophenol + 2-deoxy-alpha-D-glucose
4-nitrophenyl 3-deoxy-alpha-D-glucopyranoside + H2O
4-nitrophenol + 3-deoxy-alpha-D-glucose
very low activity, wild-type and recombinant enzyme
-
-
?
4-nitrophenyl alpha-D-galactopyranoside + H2O
4-nitrophenol + alpha-D-galactopyranose
-
-
-
?
4-nitrophenyl alpha-D-glucopyranosyl-1,4-alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
-
alpha-1,4-glycosidic bond
-
-
?
4-nitrophenyl alpha-glucopyranoside + H2O
4-nitrophenol + alpha-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
-
-
-
?
4-nitrophenyl D-glucopyranoside + H2O
4-nitrophenol + alpha-glucopyranose
-
-
-
-
?
4-O-alpha-D-glucopyranosyl-D-fructose + H2O
alpha-D-glucose + D-fructose
-
-
-
?
4-O-alpha-D-glucopyranosyl-D-glucopyranose + H2O
alpha-D-glucose + alpha-D-glucose
-
-
-
?
4-O-alpha-D-glucopyranosyl-D-sorbitol + H2O
alpha-D-glucose + D-sorbitol
-
-
-
?
5-O-alpha-D-glucopyranosyl-D-fructose + H2O
alpha-D-glucose + D-fructose
-
-
-
?
6-O-alpha-D-glucopyranosyl-D-fructofuranoside + H2O
alpha-D-glucose + D-fructose
-
-
-
?
alpha-cyclodextrin + H2O
alpha-D-glucose
-
low activity with isozymes MG4 and MG6
-
-
?
D-glucose + ethanol
ethyl-alpha-D-glucoside
-
transglucosylation activity in presence of ethanol with several substrates, e.g. maltose, kojibiose, nigerose, glycogen, starch, overview, the enzyme favors the forward reaction
-
-
r
D-glucose + maltose
maltotriose
-
transglycosylation activity
-
-
r
dextrin + H2O
alpha-D-glucose + ?
a mixture of shorter linear and branched dextrin chains is hydrolyzed at the nonreducing ends into glucose
-
-
?
dextrin + H2O
D-glucose + ?
assay at 60°C
-
-
?
dextrin 10 + H2O
alpha-D-glucose
27% of the activity with maltose
-
-
?
glycogen + H2O
?
-
assay at 65°C, pH 5.0, reaction stopped with Na2CO3
-
-
?
isomaltosaccharides + H2O
alpha-D-glucose
-
hydrolysis of alpha-1,6-glycosidic bond of the nonreducing terminal unit
-
-
?
isomaltose
isomaltotriose + alpha-D-glucose
-
-
transglucosylation products
?
kojibiose + maltose
4-O-alpha-kojibiosyl-D-glucose + D-glucose
-
transglycosylation activity
-
-
?
L-ascorbic acid alpha-D-glucoside + H2O
maltose + L-ascorbic acid
-
-
-
-
r
maltooligosaccharide + H2O
?
the enzyme shows highest specificity for maltose and decreasing values of catalytic efficiency (kcat/Km) toward higher maltooligosaccahrides. AglA specifically liberates glucose from the non-reducing end
-
-
?
melizitose + H2O
?
-
activity with maltase, no activity with alpha-glucosidase
-
-
?
methyl alpha-D-glucopyranoside + H2O
methanol + alpha-D-glucopyranose
-
-
-
-
?
nigerose + maltose
4-O-alpha-nigerosyl-D-glucose + D-glucose
-
transglycosylation activity
-
-
?
oligomaltose + H2O
D-glucose
broad ability in transglycosylation activity on nonsugar acceptors
-
-
?
oligosaccharides + H2O
alpha-D-glucose
-
various substrates, enzyme is exo-acting to release alpha-D-glucose, preferential cleavage of the alpha-1,4-bond
-
-
?
p-aminophenyl-alpha-D-glucoside + H2O
alpha-D-glucose + 4-aminophenol
-
-
-
-
?
p-nitrophenyl alpha-D-glucopyranoside
4-nitrophenol + D-glucose
-
assay at pH 6.8, 37°C
-
-
?
p-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
assay at pH 6.8, 37°C, reaction stopped by adding Na2CO3
-
-
?
p-nitrophenyl alpha-D-glucopyranoside + H2O
? + p-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
p-nitrophenyl-alpha-D-maltoside + H2O
p-nitrophenol + alpha-D-maltose
-
-
-
?
panose
alpha-D-glucose + tetrasaccharides
-
-
transglucosylation products
?
panose + H2O
alpha-D-glucopyranose + alpha-D-glucopyranosyl-1,4-alpha-D-glucopyranosyl-1,6-alpha-D-glucopyranosyl-1,4-D-glucopyranose
-
hydrolysis of alpha-1,6-glycosidic bond of the nonreducing terminal unit
-
-
?
phenyl alpha-maltoside + H2O
alpha-D-glucose + ?
preferred substrate, stereospecific production of alpha-D-glucose which spontaneously mutarotates to beta-glucose
-
-
?
resorufin alpha-D-glucopyranoside + H2O
?
-
assay at room temperature, 10 min incubation, 7.4 nM enzyme concentration
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
-
hydrolysis of alpha-1,2-glycosidic bond of the nonreducing terminal unit
-
-
?
1,4-alpha-D-glucooligosaccharide + H2O
alpha-D-glucose
-
short glucose oligomers, substrate derived from starch by alpha-amylase activity, the enzyme is important in mucosal alpha-glucogenesis, MGAM primes and mucosal sucrase-isomaltase activity sustains and constrains prandial alpha-glucogenesis from starch oligomers, regulation mechanism, overview
-
-
?
1,4-alpha-D-glucooligosaccharide + H2O
alpha-D-glucose
-
short glucose oligomers, substrate derived from starch
-
-
?
1,4-alpha-D-glucooligosaccharide + H2O
alpha-D-glucose
the four isozymes digest all linear starch oligosaccharides to glucose
-
-
?
4-methylumbelliferyl alpha-D-glucopyranoside + H2O
4-methylumbelliferol + alpha-D-glucopyranose
-
-
-
-
?
4-methylumbelliferyl alpha-D-glucopyranoside + H2O
4-methylumbelliferol + alpha-D-glucopyranose
-
-
-
-
?
4-methylumbelliferyl alpha-D-glucopyranoside + H2O
4-methylumbelliferol + alpha-D-glucopyranose
-
-
-
-
?
4-methylumbelliferyl alpha-D-glucopyranoside + H2O
4-methylumbelliferone + alpha-D-glucopyranose
-
-
-
?
4-methylumbelliferyl alpha-D-glucopyranoside + H2O
4-methylumbelliferone + alpha-D-glucopyranose
-
-
-
?
4-methylumbelliferyl-alpha-D-glucopyranoside + H2O
4-methylumbelliferol + alpha-D-glucose
-
-
-
-
?
4-methylumbelliferyl-alpha-D-glucopyranoside + H2O
4-methylumbelliferol + alpha-D-glucose
-
-
-
-
?
4-methylumbelliferyl-alpha-D-glucopyranoside + H2O
4-methylumbelliferol + alpha-D-glucose
-
-
-
-
?
4-methylumbelliferyl-alpha-D-glucopyranoside + H2O
4-methylumbelliferol + alpha-D-glucose
-
-
-
-
?
4-methylumbelliferyl-alpha-D-glucopyranoside + H2O
4-methylumbelliferone + alpha-D-glucose
assay at pH 7.0, 37°C, 30 min incubation
-
-
?
4-methylumbelliferyl-alpha-D-glucopyranoside + H2O
4-methylumbelliferone + alpha-D-glucose
assay at pH 4.0, 37°C, reaction stopped by addition of glycine or sodium carbonate
-
-
?
4-methylumbelliferyl-alpha-D-glucopyranoside + H2O
4-methylumbelliferone + alpha-D-glucose
-
assay at room temperature, 10 min incubation, 7.4 nM enzyme concentration
-
-
?
4-methylumbelliferyl-alpha-glucoside + H2O
4-methylumbelliferone + alpha-D-glucose
-
-
-
-
?
4-methylumbelliferyl-alpha-glucoside + H2O
4-methylumbelliferone + alpha-D-glucose
-
-
-
-
?
4-methylumbelliferyl-alpha-glucoside + H2O
4-methylumbelliferone + alpha-D-glucose
-
4-methylumbelliferyl alpha-D-glucopyranoside
-
-
?
4-methylumbelliferyl-alpha-glucoside + H2O
4-methylumbelliferone + alpha-D-glucose
-
-
-
-
?
4-methylumbelliferyl-alpha-glucoside + H2O
4-methylumbelliferone + alpha-D-glucose
-
-
-
-
?
4-methylumbelliferyl-alpha-glucoside + H2O
4-methylumbelliferone + alpha-D-glucose
-
-
-
-
?
4-methylumbelliferyl-alpha-glucoside + H2O
4-methylumbelliferone + alpha-D-glucose
-
-
-
-
?
4-nitrophenyl 2-deoxy-alpha-D-glucopyranoside + H2O
4-nitrophenol + 2-deoxy-alpha-D-glucose
low activity, wild-type and recombinant enzyme
-
-
?
4-nitrophenyl 2-deoxy-alpha-D-glucopyranoside + H2O
4-nitrophenol + 2-deoxy-alpha-D-glucose
low activity, wild-type and recombinant enzyme
-
-
?
4-nitrophenyl 2-deoxy-alpha-D-glucopyranoside + H2O
4-nitrophenol + 2-deoxy-alpha-D-glucose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
high activity
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
Saccharolobus solfataricus MT-4 / DSM 5833
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
preferred substrate
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
preferred substrate
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
very low activity, wild-type and recombinant enzyme
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
very low activity, wild-type and recombinant enzyme
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
-
preferred substrate
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
-
preferred substrate
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
assay at pH 7.5, 37°
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
low activity
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
-
assay at pH 6.8
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
Alkalihalophilus pseudofirmus
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
Alkalihalophilus pseudofirmus 703
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
assay at pH 5.5, 50°C, reaction terminated by sodium carbonate solution
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
assay at 65°C, pH 5.0, reaction stopped with Na2CO3
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
assay at 60°C
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
assay at pH 5.0, 37°C, reaction stopped by adding sodium carbonate
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
assay at pH 6.8, 37°C, reaction stopped by adding of NaOH
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
assay at pH 5.5, 30°C
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl alpha-D-glucoside
4-nitrophenol + alpha-D-glucose
-
-
-
-
?
4-nitrophenyl alpha-D-glucoside + H2O
4-nitrophenol + alpha-D-glucose
-
-
-
-
?
4-nitrophenyl alpha-D-glucoside + H2O
4-nitrophenol + alpha-D-glucose
-
-
-
?
4-nitrophenyl alpha-D-glucoside + H2O
4-nitrophenol + alpha-D-glucose
-
-
-
?
4-nitrophenyl alpha-D-glucoside + H2O
4-nitrophenol + D-glucose
low activity
-
-
?
4-nitrophenyl alpha-D-glucoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl alpha-D-glucoside + H2O
4-nitrophenol + D-glucose
-
assay at pH 6.0, 30°C
-
-
?
4-nitrophenyl alpha-D-mannopyranoside + H2O
4-nitrophenol + alpha-D-mannopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-mannopyranoside + H2O
4-nitrophenol + alpha-D-mannopyranose
-
-
-
-
?
amylopectin + H2O
?
-
assay at 65°C, pH 5.0, reaction stopped with Na2CO3
-
-
?
amylopectin + H2O
D-glucose + ?
Alkalihalophilus pseudofirmus
from maize, best substrate
-
-
?
amylopectin + H2O
D-glucose + ?
Alkalihalophilus pseudofirmus 703
from maize, best substrate
-
-
?
amylose + H2O
alpha-D-glucose
-
low activity with alpha-glucosidase Ia and IIa, only traces of activity with alpha-glucosidase Ib and IIb
-
-
?
glycogen + H2O
alpha-D-glucose
-
activity with acid alpha-glucosidase I and II, no activity with neutral alpha-glucosidase
-
-
?
isomaltose + H2O
2 alpha-D-glucose
-
high activity with alpha-glucosidase III, very low activity with alpha-glucosidase I and II
-
-
?
isomaltose + H2O
2 alpha-D-glucose
-
activity with alpha-glucosidase, no activity with maltase
-
-
?
isomaltose + H2O
2 alpha-D-glucose
-
maltase shows low activity with isomaltose, alpha-glucosidase shows high activity
-
-
?
isomaltose + H2O
2 alpha-D-glucose
-
hydrolysis of the alpha-1,6-glycosidic bond
-
-
?
isomaltose + H2O
2 alpha-D-glucose
-
hydrolyzed by alpha-maltosidase I, no activity with alpha-glucosidase II and III
-
-
?
isomaltose + H2O
2 alpha-D-glucose
-
-
-
?
isomaltose + H2O
2 D-glucose
hydrolysis of alpha-1,6-bond
-
-
?
isomaltose + H2O
2 D-glucose
hydrolyzed to e lesser extent than maltose
-
-
?
isomaltose + H2O
?
preferred substrate for strain GK24 and HB8
-
-
?
isomaltose + H2O
?
preferred substrate for strain GK24 and HB8
-
-
?
isomaltose + H2O
alpha-D-glucose + D-glucose
-
-
-
-
?
isomaltose + H2O
alpha-D-glucose + D-glucose
i.e. alpha-D-Glc-(1->6)-D-Glc
-
-
?
isomaltotriose + H2O
alpha-D-glucose
-
activity with alpha-glucosidase, no activity with maltase
-
-
?
isomaltotriose + H2O
alpha-D-glucose
-
-
-
?
kojibiose + H2O
2 D-glucose
hydrolyzed to e lesser extent than maltose
-
-
?
kojibiose + H2O
alpha-D-glucose + D-glucose
-
-
-
-
?
kojibiose + H2O
alpha-D-glucose + D-glucose
-
hydrolysis of the alpha-1,2-glycosidic bond
-
-
?
kojibiose + H2O
alpha-D-glucose + D-glucose
-
hydrolysis of the alpha-1,2-glycosidic bond
-
-
?
kojibiose + H2O
alpha-D-glucose + D-glucose
low activity
-
-
?
kojibiose + H2O
alpha-D-glucose + D-glucose
i.e. alpha-D-Glc-(1->2)-D-Glc
-
-
?
kojibiose + H2O
alpha-D-glucose + D-glucose
i.e. alpha-D-Glc-(1->2)-D-Glc
-
-
?
kojibiose + H2O
alpha-D-glucose + D-glucose
-
low activity with alpha-glucosidase Ia and IIa, only traces of activity with alpha-glucosidase Ib and IIb
-
-
?
malto-oligosaccharides + H2O
alpha-D-glucose
-
-
-
-
?
malto-oligosaccharides + H2O
alpha-D-glucose
-
from starch
-
-
?
malto-oligosaccharides + H2O
alpha-D-glucose
-
-
-
-
?
malto-oligosaccharides + H2O
alpha-D-glucose
-
from starch
-
-
?
maltohexaose + H2O
maltopentaose + D-glucose
-
-
-
-
?
maltooligosaccharides + H2O
alpha-D-glucose
-
-
-
-
?
maltopentaose + H2O
D-glucose + ?
assay at 60°C
-
-
?
maltose
panose + ?
-
-
alpha-glucosyltransfer products: panose + isomaltose
?
maltose
panose + ?
-
-
alpha-glucosyltransfer products: panose + isomaltose
?
maltose + H2O
2 D-glucose
hydrolysis of alpha-1,4-bond
-
-
?
maltose + H2O
2 D-glucose
-
hydrolysis of the alpha-1,4-glycosidic bond
-
-
?
maltose + H2O
2 D-glucose
-
hydrolysis of the alpha-1,4-glycosidic bond
-
-
?
maltose + H2O
2 D-glucose
-
maltose is a glucosyl donor for transglycosylation activity, high activity
-
-
?
maltose + H2O
2 D-glucose
-
maltose is a glucosyl donor for transglycosylation activity, high activity
-
-
?
maltose + H2O
2 D-glucose
-
assay at pH 6.9, 37°C, reaction stopped by suspension of the mixtures in boiling water for 10 min
-
-
?
maltose + H2O
?
-
assay at 65°C, pH 5.0, reaction stopped with Na2CO3
-
-
?
maltose + H2O
?
alpha-1,4 linkage, poor substrate. Enzyme can hydrolyze maltose but only at higher substrate and enzyme concentrations
-
-
?
maltose + H2O
?
alpha-1,4 linkage, poor substrate. Enzyme can hydrolyze maltose but only at higher substrate and enzyme concentrations
-
-
?
maltose + H2O
alpha-D-glucose + D-glucose
preferred substrate of wild-type and recombinant enzyme
-
-
?
maltose + H2O
alpha-D-glucose + D-glucose
preferred substrate of wild-type and recombinant enzyme
-
-
?
maltose + H2O
alpha-D-glucose + D-glucose
-
activity with maltase, no activity with alpha-glucosidase
-
-
?
maltose + H2O
alpha-D-glucose + D-glucose
-
maltase hydrolyzes maltose preferentially
-
-
?
maltose + H2O
alpha-D-glucose + D-glucose
-
-
-
-
?
maltose + H2O
alpha-D-glucose + D-glucose
-
-
-
-
?
maltose + H2O
alpha-D-glucose + D-glucose
-
preferred substrate of isozymes MG4 and MG6
-
-
?
maltose + H2O
alpha-D-glucose + D-glucose
-
-
-
-
?
maltose + H2O
alpha-D-glucose + D-glucose
probable physiological role of the enzyme in the utilization of exogenous glycoproteins and/or in the turnover of the organisms own glycoproteins, overview
-
-
?
maltose + H2O
alpha-D-glucose + D-glucose
preferred substrate, the enzyme shows strict glucose substrate specificity hydrolyzing maltose, as well as longer alpha-1,4-linked maltooligosaccharides
-
-
?
maltose + H2O
alpha-D-glucose + D-glucose
-
-
-
-
?
maltose + H2O
alpha-D-glucose + D-glucose
preferred substrate, Asp251 and Trp284 interact with the position 6 OH group of the substrate
-
-
?
maltose + H2O
alpha-D-glucose + D-glucose
-
hydrolyzed by alpha-glucosidase II and III, no activity with alpha-glucosidase I
-
-
?
maltose + H2O
alpha-D-glucose + D-glucose
the enzyme is involved in maltose and starch metabolism
-
-
?
maltose + H2O
alpha-D-glucose + D-glucose
-
-
-
?
maltose + H2O
alpha-D-glucose + D-glucose
-
-
-
?
maltose + H2O
alpha-D-glucose + D-glucose
Thermochaetoides thermophila
-
preferred substrate
-
-
?
maltose + H2O
alpha-D-glucose + D-glucose
-
preferred substrate of both isozymes
-
-
?
maltose + H2O
D-glucose + ?
assay at 60°C
-
-
?
maltotetraose + H2O
alpha-D-glucose
54% of the activity with maltose
-
-
?
maltotetraose + H2O
D-glucose + ?
assay at 60°C
-
-
?
maltotriose + 2 H2O
3 D-glucose
44% of the activity with maltose
-
-
?
maltotriose + 2 H2O
3 D-glucose
44% of the activity with maltose
-
-
?
maltotriose + H2O
?
poor substrate. Enzyme can hydrolyze maltotriose but only at higher substrate and enzyme concentrations
-
-
?
maltotriose + H2O
?
poor substrate. Enzyme can hydrolyze maltotriose but only at higher substrate and enzyme concentrations
-
-
?
maltotriose + H2O
alpha-D-glucose + ?
-
highest activity
-
-
?
maltotriose + H2O
D-glucose + ?
assay at 60°C
-
-
?
maltotriose + H2O
maltose + D-glucose
-
activity with maltase, no activity with alpha-glucosidase
-
-
?
maltotriose + H2O
maltose + D-glucose
-
hydrolyzed by alpha-glucosidase II and III, no activity with alpha-glucosidase I
-
-
?
methyl-alpha-glucoside + H2O
methanol + alpha-D-glucose
-
no activity
-
-
?
methyl-alpha-glucoside + H2O
methanol + alpha-D-glucose
-
phenyl-alpha-glucopyranoside
-
-
?
methyl-alpha-glucoside + H2O
methanol + alpha-D-glucose
-
phenyl-alpha-glucopyranoside
-
-
?
methyl-alpha-glucoside + H2O
methanol + alpha-D-glucose
-
hydrolysis with alpha-glucosidase I, no activity with alpha-glucosidase II and III
-
-
?
nigerose + H2O
2 alpha-D-glucose
-
best substrate, hydrolysis of the alpha-1,3-glycosidic bond
-
-
?
nigerose + H2O
2 alpha-D-glucose
-
best substrate, hydrolysis of the alpha-1,3-glycosidic bond
-
-
?
nigerose + H2O
2 alpha-D-glucose
-
alpha-1,3-linkage, exists as abnormal linkage in starch
-
-
?
nigerose + H2O
2 alpha-D-glucose
-
hydrolyzed by alpha-glucosidase II and III, no activity with alpha-glucosidase I
-
-
?
nigerose + H2O
2 alpha-D-glucose
-
hydrolysis of alpha-1,3-glycosidic bond of the nonreducing terminal unit
-
-
?
nigerose + H2O
2 alpha-D-glucose
-
hydrolysis of alpha-1,3-glycosidic bond of the nonreducing terminal unit
-
-
?
nigerose + H2O
2 D-glucose
hydrolyzed to e lesser extent than maltose
-
-
?
nigerose + H2O
alpha-D-glucose + D-glucose
alpha-1,3-linkage, very low activity
-
-
?
nigerose + H2O
alpha-D-glucose + D-glucose
i.e. alpha-D-Glc-(1->3)-D-Glc
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
p-nitrophenyl-alpha-D-glucopyranoside
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
high activity with alpha-glucosidase, no activity with maltase
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
p-nitrophenyl-alpha-D-glucopyranoside
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
maltase shows low activity with p-nitrophenyl-alpha-D-glucopyranoside, alpha-glucosidase shows high activity
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
p-nitrophenyl-alpha-D-glucopyranoside
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
p-nitrophenyl-alpha-D-glucopyranoside
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
no activity
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
p-nitrophenyl-alpha-D-glucopyranoside
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
p-nitrophenyl-alpha-D-glucopyranoside
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
p-nitrophenyl-alpha-D-glucopyranoside
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
p-nitrophenyl-alpha-D-glucopyranoside
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
best substrate
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
best substrate
-
-
?
panose + H2O
maltose + alpha-D-glucose
alpha-D-Glc-(1->6)-alpha-D-Glc-(1->4)-D-Glc
-
-
?
phenyl alpha-D-glucoside + H2O
phenol + alpha-D-glucose
-
phenyl-alpha-glucopyranoside
-
-
?
phenyl alpha-D-glucoside + H2O
phenol + alpha-D-glucose
-
phenyl-alpha-glucopyranoside
-
-
?
phenyl alpha-D-glucoside + H2O
phenol + alpha-D-glucose
-
-
-
-
?
phenyl alpha-glucoside + H2O
alpha-D-glucose + phenol
low activity
-
-
?
phenyl alpha-maltoside + H2O
alpha-D-glucose + phenyl alpha-D-glucoside
-
-
-
-
?
phenyl alpha-maltoside + H2O
alpha-D-glucose + phenyl alpha-D-glucoside
-
-
-
?
phenyl alpha-maltoside + H2O
alpha-D-glucose + phenyl alpha-D-glucoside
-
-
-
?
phenyl alpha-maltoside + H2O
alpha-D-glucose + phenyl alpha-D-glucoside
-
-
-
?
phenyl alpha-maltoside + H2O
alpha-D-glucose + phenyl alpha-D-glucoside
-
-
-
?
phenyl alpha-maltoside + H2O
alpha-D-glucose + phenyl alpha-D-glucoside
-
-
alpha-D-glucose + ?
?
phenyl alpha-maltoside + H2O
alpha-D-glucose + phenyl alpha-D-glucoside
-
-
-
?
phenyl alpha-maltoside + H2O
alpha-D-glucose + phenyl alpha-D-glucoside
-
hydrolyzed by alpha-glucosidase II and III, no activity with alpha-glucosidase I
-
-
?
phenyl alpha-maltoside + H2O
alpha-D-glucose + phenyl alpha-D-glucoside
-
-
-
?
phenyl alpha-maltoside + H2O
alpha-D-glucose + phenyl alpha-D-glucoside
-
-
-
?
RS toxin + H2O
?
-
specific for the host-specific Rhizoctonia solani toxin, purified from Rhizoctonia solani-inoculated rice sheath, inactivation of the toxin and inhibition of the fungal mycelial growth
-
-
?
RS toxin + H2O
?
-
host-specific Rhizoctonia solani toxin, purified from Rhizoctonia solani-inoculated rice sheath, inactivation of the toxin, preferred substrate
-
-
?
RS toxin + H2O
?
-
specific for the host-specific Rhizoctonia solani toxin, purified from Rhizoctonia solani-inoculated rice sheath, inactivation of the toxin and inhibition of the fungal mycelial growth
-
-
?
RS toxin + H2O
?
-
host-specific Rhizoctonia solani toxin, purified from Rhizoctonia solani-inoculated rice sheath, inactivation of the toxin, preferred substrate
-
-
?
soluble starch + H2O
?
Alkalihalophilus pseudofirmus
76.2% activity compared to amylopectin
-
-
?
soluble starch + H2O
?
Alkalihalophilus pseudofirmus 703
76.2% activity compared to amylopectin
-
-
?
soluble starch + H2O
alpha-D-glucose
-
the enzyme hydrolyzes alpha-1,4-glycosidic bonds, exo-acting enzyme
-
-
?
starch + H2O
?
-
assay at 65°C, pH 5.0, reaction stopped with Na2CO3
-
-
?
starch + H2O
alpha-D-glucose
-
no activity with maltase or alpha-glucosidase
-
-
?
starch + H2O
alpha-D-glucose
one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion
-
-
?
starch + H2O
alpha-D-glucose
-
soluble starch, high activity, best substrate
-
-
?
sucrose + H2O
D-fructose + alpha-D-glucose
-
activity with maltase, no activity with alpha-glucosidase
-
-
?
sucrose + H2O
D-fructose + alpha-D-glucose
-
hydrolyzed by alpha-glucosidase II and III, no activity with alpha-glucosidase I
-
-
?
sucrose + H2O
D-fructose + D-glucose
alpha-1,2 linkage
-
-
?
sucrose + H2O
D-fructose + D-glucose
Thermus thermophilus HB27 HB27 / ATCC BAA-163 / DSM 7039
alpha-1,2 linkage
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
assay at pH 6.9, 37°C, reaction stopped by suspension of the mixtures in boiling water for 10 min
-
-
?
trehalose + H2O
?
-
hydrolysis of the alpha-1,1-glycosidic bond
-
-
?
trehalose + H2O
alpha-D-glucose
site-specific GK24 alpha-glucosidase mutant, Vmax: 20 micromol/min mg
-
-
?
turanose + H2O
alpha-D-glucose + D-fructose
-
hydrolyzed by alpha-glucosidase II and III, no activity with alpha-glucosidase I
-
-
?
turanose + H2O
alpha-D-glucose + D-fructose
-
hydrolysis of alpha-1,3-glycosidic bond of the nonreducing terminal unit
-
-
?
turanose + H2O
alpha-D-glucose + D-fructose
-
hydrolysis of alpha-1,3-glycosidic bond of the nonreducing terminal unit
-
-
?
additional information
?
-
Alkalihalophilus pseudofirmus
the alpha-glucosidase (EC 3.2.1.20) from Bacillus pseudofirmus strain 703 also shows oligo-alpha-1,6-glucosidase activity (EC 3.2.1.10), having both exo-alpha-1,4-glucosidase and oligo-l,6-glucosidase activities, but it shows no transglycosylation activity. The enzyme exhibits high activity against amylopectin from maize and soluble starch, but no activity against amylose from potato, pullulan, carboxymethylcellulose, and beachwood xylan. Amy112 hydrolyzes alpha-1,6-glucosidic linkages less effective than alpha-1,4-glucosidic linkages. Hydrolysates of amylopectin from maize, maltose, and maltotriose are mainly glucose
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additional information
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Alkalihalophilus pseudofirmus 703
the alpha-glucosidase (EC 3.2.1.20) from Bacillus pseudofirmus strain 703 also shows oligo-alpha-1,6-glucosidase activity (EC 3.2.1.10), having both exo-alpha-1,4-glucosidase and oligo-l,6-glucosidase activities, but it shows no transglycosylation activity. The enzyme exhibits high activity against amylopectin from maize and soluble starch, but no activity against amylose from potato, pullulan, carboxymethylcellulose, and beachwood xylan. Amy112 hydrolyzes alpha-1,6-glucosidic linkages less effective than alpha-1,4-glucosidic linkages. Hydrolysates of amylopectin from maize, maltose, and maltotriose are mainly glucose
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additional information
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an exo-acting glycoside hydrolase, that catalyzes the hydrolysis of alpha-glucosyl residues from the non-reducing end of alpha-linked substrates to release alpha-glucose, 4-nitrophenyl-alpha-D-maltopentaoside, 4-nitrophenyl-beta-D-galactopyranoside, and 4-nitrophenyl-alpha-D-galactopyranoside are poor substrates, overview
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additional information
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the enzyme shows a wide substrate specificity cleaving alpha-(1,1)-, alpha-(1,2)-, alpha-(1,4)- and alpha-(1,6)-glucosidic linkages, and rapidly hydrolyzing 4-nitrophenyl alpha-D-glucoside alpha-(1,6) and sucrose alpha-(1,2) linkages. Recombinant and native display positive cooperativity to sucrose, turanose alpha-(1,3), kojibiose alpha-(1,2) and soluble starch alpha-(1,4), the recombinant His-tagged enzyme hydrolyzes isomaltose and soluble starch but with different Km values
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additional information
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no activity toward isomaltose, nigerose or soluble starch
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?
additional information
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substrate specificity, overview, the enzyme is also active with sucrose and turanose
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?
additional information
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maltooligosachharides of four or more units of polymerization are slowly hydrolyzed
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additional information
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substrate aglycon specificity profiling, overview
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additional information
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no activity in hydrolysis with starch, panose, pullulan, amylopectin, amylose, isomaltose, and saccharose, the enzyme also performs transglycosylation reactions with different donors and a variety of acceptors, product determinations, the activity with alpha-1,4-glycosidic linkages is higher compared to alpha-1,6-glycosidic likanges, substrate specificity, overview
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additional information
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the enzyme shows strong transglycosylation activity
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additional information
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the enzyme shows strong transglycosylation activity
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additional information
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the enzyme shows strong transglycosylation activity
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additional information
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no activity of wild-type and recombinant enzyme with 4-nitrophenyl 4-deoxy-alpha-D-glucopyranoside and 4-nitrophenyl 6-deoxy-alpha-D-glucopyranoside
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additional information
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substrate aglycon specificity profiling, overview
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additional information
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immobilized recombinant alpha-glucosidase catalyzes maltose into isomaltooligosaccharides (IMOs) by its transglucosylation activity. The synthesis of IMOs is conducted using maltose as the substrate
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additional information
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synthesis of panose or isomaltose by transglycosylation as a function of the glucosyl acceptor, panose is the main transglycosylation product after 8 h of incubation, whereas isomaltose is predominant after 24 h. Isomaltose also becomes predominant at shorter times if a mixture of maltose and glucose is used instead of maltose
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additional information
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the recombinant enzyme performs isomaltooligosaccharides (IMOs) synthesis by transglycosylation. Quantitative analyses of products maltose (M), isomaltose (IG2), panose (P), and isomaltotriose (IG3)
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additional information
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transglucosylation activity by wild-type and Asn694 mutant enzymes forming isomaltooligosaccharides, overview. Isomaltose and panose are the predominant final products of wild-type alpha-glucosidase
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additional information
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no activity of wild-type and recombinant enzyme with 4-nitrophenyl 4-deoxy-alpha-D-glucopyranoside and 4-nitrophenyl 6-deoxy-alpha-D-glucopyranoside
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additional information
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the enzyme has a function in endogenous metabolism of alpha-glucans provided extracellularly as carbon source
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additional information
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the formation of maltase and alpha-glucosidase is induced by trehalose, sucrose or lactose in the growth medium
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additional information
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transglucosylation activity with isomaltose and maltotriose
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additional information
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maltase shows no transglucosylation activity, alpha-glucosidase shows transglucosidase activity with isomaltose or maltotriose
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additional information
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optimal enzyme production reaches a maximum after 24 h growth
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additional information
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the enzyme is a specific oligo-1,4-1,6-alpha-glucosidase
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additional information
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maltose is required for induction. The enzyme may play a role in the breakdown of internal storage polysaccharides containing alpha-1,4 and alpha-1,6 bonds
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additional information
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expression is subject to both maltose induction and carbon catabolite repression. Induction of enzyme expression also occurs when starch, amylose, or glycogen are present in the growth medium
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additional information
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no activity with sucrose and trehalose, poor activity with isomaltose
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?
additional information
?
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no activity with sucrose and trehalose, poor activity with isomaltose
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?
additional information
?
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the enzyme might be mainly responsible for the predominant formation of glucose in starch hydrolysis of the germinating beet endosperm
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additional information
?
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substrate aglycon specificity profiling, overview
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additional information
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the enzyme is able to hydrolyze alpha-1,2, alpha-1,3, alpha-1,4, and alpha-1,6 glycosidic O-linkages and liberates alpha-D-glucose from the non-reducing end of substrates
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additional information
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the enzyme is not able to hydrolyze polysaccharides, such as amylose, amylopectin, starch, or alpha-, beta-, and gamma-cyclodextrin
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additional information
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the enzyme is able to hydrolyze alpha-1,2, alpha-1,3, alpha-1,4, and alpha-1,6 glycosidic O-linkages and liberates alpha-D-glucose from the non-reducing end of substrates
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?
additional information
?
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the enzyme is not able to hydrolyze polysaccharides, such as amylose, amylopectin, starch, or alpha-, beta-, and gamma-cyclodextrin
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?
additional information
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the enzyme is able to incorporate tracer quantities of alpha-D-glucose into glycogen starting either from alpha-D-glucose or maltose
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?
additional information
?
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enzymic digestion profile determination for camel small intestine, overview
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?
additional information
?
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poor activity with sucrose, dextrine, lactose, and no activity with xylose
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?
additional information
?
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the enzyme shows no ability to bind to or digest raw starch
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?
additional information
?
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the enzyme shows no ability to bind to or digest raw starch
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?
additional information
?
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the enzyme has a role in the general carbohydrate metabolism, and in glycoprotein processing
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?
additional information
?
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no activity with trehalose, kojibiose, and cellobiose
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?
additional information
?
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the enzyme has a role in the general carbohydrate metabolism, and in glycoprotein processing
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?
additional information
?
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no activity with trehalose, kojibiose, and cellobiose
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?
additional information
?
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no activity with cellobiose
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?
additional information
?
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an essential cysteine residue is present at the active site. Members of GH4 employ a unique catalytic mechanism for cleavage of the glycosidic bond. GH4 single or double-displacement mechanism
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?
additional information
?
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an essential cysteine residue is present at the active site. Members of GH4 employ a unique catalytic mechanism for cleavage of the glycosidic bond. GH4 single or double-displacement mechanism
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?
additional information
?
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an essential cysteine residue is present at the active site. Members of GH4 employ a unique catalytic mechanism for cleavage of the glycosidic bond. GH4 single or double-displacement mechanism
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additional information
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induced by maltose but repressed by alpha-D-glucose and fructose
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additional information
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the enzyme also shows high transglycosylation activity, it transfers glucosyl groups from maltose to produce maltotriose selectively
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?
additional information
?
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the enzyme also shows high transglycosylation activity, it transfers glucosyl groups from maltose to produce maltotriose selectively
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additional information
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the enzyme also shows high transglycosylation activity, it transfers glucosyl groups from maltose to produce maltotriose selectively
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additional information
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451 thermophilic bacilli are isolated and 67 isolates with a high amylase activity are selected to determine the alpha-glucosidase production capacities. alpha-Glucosidase production capacities of the isolates vary within the range from 77.18 to 0.001 U/g
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additional information
?
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substrate aglycon specificity profiling, overview
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?
additional information
?
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the enzyme specifically hydrolyzes alpha-1,4-glucosidic bonds in maltose, maltooligosaccharides, and alpha-glucans, isomaltose is a poor substrate, residues Ala200 and Asn258 in the conserved region II and III, respectively, are largely responsible for substrate recognition
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additional information
?
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alpha-glucosidases play important roles in the digestion of carbohydrates and biosynthesis of viral envelope glycoproteins
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additional information
?
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biotransformation of starch using the alpha-transglucosidase-producing Geobacillus stearothermophilus U2
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additional information
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biotransformation of starch using the alpha-transglucosidase-producing Geobacillus stearothermophilus U2
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additional information
?
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the enzyme specifically hydrolyzes alpha-1,4-glucosidic bonds in maltose, maltooligosaccharides, and alpha-glucans, isomaltose is a poor substrate, residues Ala200 and Asn258 in the conserved region II and III, respectively, are largely responsible for substrate recognition
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additional information
?
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biotransformation of starch using the alpha-transglucosidase-producing Geobacillus stearothermophilus U2
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additional information
?
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biotransformation of starch using the alpha-transglucosidase-producing Geobacillus stearothermophilus U2
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?
additional information
?
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strain HRO10 alpha-amylase and alpha-glucosidase show an excellent synergistic action and do not reveal any transglycosylation catalyzed reaction by the alpha-glucosidase
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?
additional information
?
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strain HRO10 alpha-amylase and alpha-glucosidase show an excellent synergistic action and do not reveal any transglycosylation catalyzed reaction by the alpha-glucosidase
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?
additional information
?
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no activity with 4-nitrophenyl alpha-D-xylopyranoside
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?
additional information
?
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no activity with 4-nitrophenyl alpha-D-xylopyranoside
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?
additional information
?
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alpha-glucosidase C releases alpha-D-glucose from glycogen as well as from low molecular weight artificial and natural substrates. alpha-glucosidase AB does not utilize alpha-1,4 linked glucose substrates larger than a disaccharide
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additional information
?
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pompe disease, glycosidosis type II, is an autosomal recessive lysosomal storage disease that results from a deficiency of acid alpha-glucosidase. Patients with this disorder are unable to break down lysosomal glycogen, which consequently accumulates in the lysosome
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additional information
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glycogen storage disease is caused by lysosomal acid alpha-glucosidase deficiency
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?
additional information
?
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a severe form of enzyme deficiency causes the infantile Pompe disease
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additional information
?
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development and evaluation of an assay method for enzyme detection in dried blood spot specimen from patients with infantile Pompe disease, overview
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?
additional information
?
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structure of the N-terminal catalytic subunit and the active site, and basis of inhibition and substrate specificity, overview, the catalytic subunit shows higher affinity for longer maltose oligosaccharides
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?
additional information
?
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the enzyme is active with maltose, maltotriose, and sucrose
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?
additional information
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transcription reaches a maximum 48 h after the start of germination
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?
additional information
?
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transcription reaches a maximum 48 h after the start of germination
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?
additional information
?
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the organism does not possess alpha-amylase activity
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?
additional information
?
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dextran, pullulan, ethyl-alpha-D-glucoside, sucrose, and trehalose are poor substrates
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?
additional information
?
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the organism does not possess alpha-amylase activity
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?
additional information
?
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dextran, pullulan, ethyl-alpha-D-glucoside, sucrose, and trehalose are poor substrates
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?
additional information
?
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synthesis of riboflavin alpha-glucoside is catalyzed by the transglucosylation activity
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?
additional information
?
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the neutral alpha-glucosidase is involved in epididymal maturation, which is different in well-fed and undernourished mice, overview
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?
additional information
?
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substrate aglycon specificity profiling, overview
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?
additional information
?
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the enzyme prefers partially degraded starch substrate from germinating millet seeds
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?
additional information
?
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the enzyme hydrolyzes polymer substrate more rapidly than maltose, substrate specificity, activity with insoluble substrates, overview
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?
additional information
?
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substrate specificity, no activity with sucrose, 4-nitrophenyl alpha-D-glucopyranoside, aryl alpha-glucoside, or isomalto-oligosaccharides, overview
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?
additional information
?
-
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the enzyme has high transglucosylation activity synthesizing oligosaccharides containing alpha-1,3- and alpha-1,2-linkages, overview, 4-nitrophenyl alpha-D-glucopyranoside and isomaltose are poor substrates, no activity with trehalose, sucrose, dextran, cellobiose, pullulan, inullin, and cyclodextrin
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?
additional information
?
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the enzyme has high transglucosylation activity synthesizing oligosaccharides containing alpha-1,3- and alpha-1,2-linkages, overview, 4-nitrophenyl alpha-D-glucopyranoside and isomaltose are poor substrates, no activity with trehalose, sucrose, dextran, cellobiose, pullulan, inullin, and cyclodextrin
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?
additional information
?
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the enzyme mainly recognizes the non-reducing end of the substrate, releasing the glucose unit. Multifunctional enzyme that catalyzes the hydrolysis of terminal alpha-1,2-linked, alpha-1,3-linked and alpha-1,4-linked glucose residues, e.g. reaction of kojibiose hydrolase
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?
additional information
?
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the enzyme mainly recognizes the non-reducing end of the substrate, releasing the glucose unit. Multifunctional enzyme that catalyzes the hydrolysis of terminal alpha-1,2-linked, alpha-1,3-linked and alpha-1,4-linked glucose residues, e.g. reaction of kojibiose hydrolase
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?
additional information
?
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the enzyme catalyzes the final step in the metabolism of carbohydrates, such as starch, to glucose for cell utilization, the oligosaccharide transport system shows high affinity for trehalose and maltose
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?
additional information
?
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sucrose is a poor or no substrate, no activity with starch
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?
additional information
?
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alpha-glucosidase C may be involved in glycogen metabolism
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?
additional information
?
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substrate aglycon specificity profiling, overview
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?
additional information
?
-
substrate specificity, overview
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?
additional information
?
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-
substrate specificity, overview
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?
additional information
?
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no activity with starch and amylose
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?
additional information
?
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Saccharolobus solfataricus MT-4 / DSM 5833
-
no activity with starch and amylose
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?
additional information
?
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no activity with isomaltose, Val216 decides the enzyme's substrate specificity
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?
additional information
?
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substrate aglycon specificity profiling, overview
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?
additional information
?
-
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alpha-glucosidases play important roles in the digestion of carbohydrates and biosynthesis of viral envelope glycoproteins
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?
additional information
?
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enzyme additionally catalyses transglucosylation of vanillyl alcohol, EC 2.4.1. The reaction is very efficient with selectivity factor 149 and occurs by a ping-pong mechanism with inhibition by glucose acceptor. At low concentration of vanillyl alcohol, one additional transglucosylation product, alpha-isomaltoside of vanillyl alcohol, is detected, indicating that vanillyl alcohol glucoside is a product of the first transglucosylation reaction and a substrate for second. The rate of isomaltoside synthesis is two orders of magnitude smaller than glucoside synthesis
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?
additional information
?
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absolute anomeric specificity for alpha-glycosidic linkages
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?
additional information
?
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the enzyme prefers short substrates, e.g. maltose and maltotriose, to longer substrates, and hydrolyzes alpha-1,4-glucosidic linkages, but also acts on alpha-1,2-, alpha-1,3-, and alpha-1,6-glucosidic linkages, substrate specificity, soluble starch is a poor substrate, the catalytic site contains three subsites, subsite affinity, overview
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?
additional information
?
-
-
enzyme exhibits transglucosidase activity
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?
additional information
?
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no activity with xyloglucan oligosaccharides, 4-nitrophenyl alpha-D-xylopyranoside, and gelatinised potato starch
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?
additional information
?
-
no activity towards cellobiose, starch and glycogen
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?
additional information
?
-
no activity towards cellobiose, starch and glycogen
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?
additional information
?
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exclusively hydrolyzes alpha-1,4-glycosidic linkages of oligosaccharides in an exo-type manner, with highest catalytic efficiency toward maltotriose. The enzyme also displays transglycosylation activity, converting maltose to isomaltose, panose, maltotriose, isomaltotriose, etc.
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?
additional information
?
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exclusively hydrolyzes alpha-1,4-glycosidic linkages of oligosaccharides in an exo-type manner, with highest catalytic efficiency toward maltotriose. The enzyme also displays transglycosylation activity, converting maltose to isomaltose, panose, maltotriose, isomaltotriose, etc.
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?
additional information
?
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enzyme has alpha-1,6-glucosidase activity and alpha-1,4-glucosidase activity
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?
additional information
?
-
-
enzyme has alpha-1,6-glucosidase activity and alpha-1,4-glucosidase activity
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?
additional information
?
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the enzyme shows a transglycosylation property, by the release of oligosaccharides after 3 h of incubation with maltose, and specificity for short maltooligosaccharides, the enzymatic activity decreases following an increase in the polymerization degree of short maltooligosaccharides, low activity with maltoheptaose, no activity with starch
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?
additional information
?
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enzyme very slowly hydrolyzes starch, dextrins (degree of polymerization 2-7) and 4-nitrophenyl-alpha-D-glucopyranoside and does not hydrolyze sucrose
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?
additional information
?
-
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enzyme very slowly hydrolyzes starch, dextrins (degree of polymerization 2-7) and 4-nitrophenyl-alpha-D-glucopyranoside and does not hydrolyze sucrose
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?
additional information
?
-
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the enzyme shows a transglycosylation property, by the release of oligosaccharides after 3 h of incubation with maltose, and specificity for short maltooligosaccharides, the enzymatic activity decreases following an increase in the polymerization degree of short maltooligosaccharides, low activity with maltoheptaose, no activity with starch
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?
additional information
?
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Thermochaetoides thermophila
-
substrate specificity, overview, no activity with trehalose, the enzyme exhibits transglycosylation activity producing trehalose and maltooligosaccharides from 5% maltose, at early stages of the transglycosylation reaction trehalose is the predominant product, while at later stages maltooligosaccharides are also accumulated
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?
additional information
?
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induced during growth on maltose and starch
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?
additional information
?
-
structural analyses of two arbutin transglucosylation products of the transglucosylation reaction with arbutin and maltose indicates that the glucose unit of maltose was transferred to the C-3 and C-6 position in the glucose moiety of arbutin
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?
additional information
?
-
substrate specificity, bulky substitutents on the aglycon side are no hindrance for hydrolysis of the glycosidic bond, no activity with cyclic maltooligosaccharides, such as alpha-, beta-, or gamma-cyclodextrin
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?
additional information
?
-
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substrate specificity, bulky substitutents on the aglycon side are no hindrance for hydrolysis of the glycosidic bond, no activity with cyclic maltooligosaccharides, such as alpha-, beta-, or gamma-cyclodextrin
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-
?
additional information
?
-
-
no activity with cellobiose, laminaribiose, trehalose, strach, pullulan, lactose, maltose, leucrose, and gentibiose
-
-
?
additional information
?
-
-
no activity with cellobiose, laminaribiose, trehalose, strach, pullulan, lactose, maltose, leucrose, and gentibiose
-
-
?
additional information
?
-
cellobiose, alpha,beta-trehalose, beta,beta-trehalose, alpha,alpha-trehalose, gentiobiose, melibiose, melizitose, trehalose-6-phosphate and raffinose are no substrates
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-
?
additional information
?
-
-
cellobiose, alpha,beta-trehalose, beta,beta-trehalose, alpha,alpha-trehalose, gentiobiose, melibiose, melizitose, trehalose-6-phosphate and raffinose are no substrates
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-
?
additional information
?
-
cellobiose, beta,beta-trehalose, gentiobiose, melibiose, melizitose, trehalose-6-phosphate and raffinose are no substrates for Thermus thermophilus
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-
?
additional information
?
-
-
cellobiose, beta,beta-trehalose, gentiobiose, melibiose, melizitose, trehalose-6-phosphate and raffinose are no substrates for Thermus thermophilus
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-
?
additional information
?
-
Thermus thermophilus HB27 HB27 / ATCC BAA-163 / DSM 7039
cellobiose, alpha,beta-trehalose, beta,beta-trehalose, alpha,alpha-trehalose, gentiobiose, melibiose, melizitose, trehalose-6-phosphate and raffinose are no substrates
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-
?
additional information
?
-
Thermus thermophilus HB27 HB27 / ATCC BAA-163 / DSM 7039
cellobiose, beta,beta-trehalose, gentiobiose, melibiose, melizitose, trehalose-6-phosphate and raffinose are no substrates for Thermus thermophilus
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-
?
additional information
?
-
cellobiose, alpha,beta-trehalose, beta,beta-trehalose, alpha,alpha-trehalose, gentiobiose, melibiose, melizitose, trehalose-6-phosphate and raffinose are no substrates
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-
?
additional information
?
-
-
substrate specificity, no activity of either isozyme with amylose and glycogen, no activity of isozyme 1 with amylopectin, starch, trehalose, panose, and lactose are a poor substrates for both isozymes, amylopectin is a poor substrate for isozyme 2
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-
?
additional information
?
-
-
substrate aglycon specificity profiling, overview
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-
?
