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Information on EC 3.2.1.20 - alpha-glucosidase and Organism(s) Hordeum vulgare and UniProt Accession Q43763

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IUBMB Comments
This single entry covers a group of enzymes whose specificity is directed mainly towards the exohydrolysis of (1->4)-alpha-glucosidic linkages, and that hydrolyse oligosaccharides rapidly, relative to polysaccharide, which are hydrolysed relatively slowly, or not at all. The intestinal enzyme also hydrolyses polysaccharides, catalysing the reactions of EC 3.2.1.3 glucan 1,4-alpha-glucosidase and, more slowly, hydrolyses (1->6)-alpha-D-glucose links.
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Hordeum vulgare
UNIPROT: Q43763
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The taxonomic range for the selected organisms is: Hordeum vulgare
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide
maltotetraose
+
3
H2O
=
4
alpha-D-glucose
+
3
=
4
Synonyms
alpha-glucosidase, maltase, neutral alpha-glucosidase, alpha-d-glucosidase, alglucosidase alfa, intestinal maltase, intestinal alpha-glucosidase, alpha-1,4-glucosidase, recombinant human gaa, alpha-glucosidase ii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acid maltase
-
-
-
-
AGL
-
-
-
-
alpha-1,4-glucosidase
-
-
-
-
alpha-D-glucosidase
-
-
-
-
alpha-glucopyranosidase
-
-
-
-
alpha-glucosidase
-
-
-
-
alpha-glucoside hydrolase
-
-
-
-
glucoinvertase
-
-
-
-
glucosidoinvertase
-
-
-
-
glucosidosucrase
-
-
-
-
high pI alpha-glucosidase
-
maltase
-
-
-
-
maltase-glucoamylase
-
-
-
-
additional information
the enzyme belongs to the alpha-glucosidase family 31
SYSTEMATIC NAME
IUBMB Comments
alpha-D-glucoside glucohydrolase
This single entry covers a group of enzymes whose specificity is directed mainly towards the exohydrolysis of (1->4)-alpha-glucosidic linkages, and that hydrolyse oligosaccharides rapidly, relative to polysaccharide, which are hydrolysed relatively slowly, or not at all. The intestinal enzyme also hydrolyses polysaccharides, catalysing the reactions of EC 3.2.1.3 glucan 1,4-alpha-glucosidase and, more slowly, hydrolyses (1->6)-alpha-D-glucose links.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-42-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
isomaltose + H2O
2 alpha-D-glucose
show the reaction diagram
-
-
-
-
?
maltoheptaose + H2O
maltohexaose + D-glucose
show the reaction diagram
-
-
-
-
?
maltohexaose + H2O
maltopentaose + D-glucose
show the reaction diagram
-
-
-
-
?
maltopentaose + H2O
alpha-D-glucose + ?
show the reaction diagram
-
-
-
-
?
maltose + H2O
2 D-glucose
show the reaction diagram
-
-
-
-
?
maltose + H2O
alpha-D-glucose + D-glucose
show the reaction diagram
maltotetraose + H2O
alpha-D-glucose
show the reaction diagram
-
-
-
-
?
maltotriose + H2O
maltose + D-glucose
show the reaction diagram
-
-
-
-
?
nigerose + H2O
2 alpha-D-glucose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
show the reaction diagram
-
-
-
-
?
trehalose + H2O
alpha-D-glucose
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
maltose + H2O
2 D-glucose
show the reaction diagram
-
-
-
-
?
maltose + H2O
alpha-D-glucose + D-glucose
show the reaction diagram
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-deoxynojirimycin
-
-
4-O-alpha-glucosyl-moranoline
-
weak inhibition
acarbose
-
-
alpha-homonojirimycin
-
strong inhibition
australine
-
-
castanospermine
-
-
conduritol B epoxide
-
-
D-glucose
-
hydrolysis of p-nitrophenyl alpha-glucoside
maltose
-
above 20 mM, substrate inhibition
miglitol
-
-
N-bromosuccinimide
-
-
N-butyl-1-deoxy-nojirimycin
-
-
N-carboxypentyl-1-deoxynojirimycin
-
-
N-cyclohexylpropyl-1-deoxynojirimycin
-
-
N-nonyl-1-deoxy-nojirimycin
-
-
Nojirimycin
-
strong inhibition
Phenylglyoxal
-
-
pyridoxal 5'-phosphate
-
-
valienamine
-
-
additional information
-
1-deoxygalactonojirimycin, kifunensine, and isofagomine are poor inhibitors
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.2
maltose
-
5.32
isomaltose
-
-
7.89
maltoheptaose
-
-
5.44
maltohexaose
-
-
2.92
maltopentaose
-
-
1.7 - 1.91
maltose
2.37
maltotetraose
-
-
1.11
maltotriose
-
-
1.29
nigerose
-
-
1.04
p-nitrophenyl alpha-glucoside
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.67
maltoheptaose
-
-
6.26
maltohexaose
-
-
7.15
maltopentaose
-
-
6.02 - 81.7
maltose
6.98
maltotetraose
-
-
6.65
maltotriose
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25.6
purified recombinant enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 4.5
hydrolysis of maltose
3.5 - 4.5
-
hydrolysis of maltose, recombinant enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
inhibition of the enzyme affects seedling growth and starch degradation, phenotype, overview
physiological function
-
the alpha-glucosidase HvAGL97 is the major endosperm enzyme catalyzing the conversion of maltose to glucose but is not required for starch degradation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AGLU_HORVU
877
0
96933
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
recombinant enzyme, gel filtration
92000
wild-type enzyme, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 100000, recombinant enzyme, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
most thermolabile at, high concentrations of sucrose protect from inactivation
393344
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
begins to denature at, at pH 4
45
-
begins to denature at, at pH 5-6
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme 25fold from Pichia pastoris by dia- and ultrafiltration, nickel affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Pichia pastoris
-
gene agl97, expression of functional His-tagged full-length enzyme in Pichia pastoris, production by high cell-density fermentation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Im, H.; Henson, C.A.
Characterization of high pI alpha-glucosidase from germinated barley seeds: substrate specificity subsite affinities and active-site residues
Carbohydr. Res.
277
145-159
1995
Hordeum vulgare
-
Manually annotated by BRENDA team
Frandsen, T.P.; Lok, F.; Mirgorodskaya, E.; Roepstorff, P.; Svensson, B.
Purification, enzymatic characterization, and nucleotide sequence of a high-isoelectric-point alpha-glucosidase from barley malt
Plant Physiol.
123
275-286
2000
Hordeum vulgare (Q43763), Hordeum vulgare
Manually annotated by BRENDA team
Muslin, E.H.; Kanikula, A.M.; Clark, S.E.; Henson, C.A.
Overexpression, purification, and characterization of a barley alpha-glucosidase secreted by Pichia pastoris
Protein Expr. Purif.
18
20-26
2000
Hordeum vulgare
Manually annotated by BRENDA team
Naested, H.; Kramhoft, B.; Lok, F.; Bojsen, K.; Yu, S.; Svensson, B.
Production of enzymatically active recombinant full-length barley high pI alpha-glucosidase of glycoside family 31 by high cell-density fermentation of Pichia pastoris and affinity purification
Protein Expr. Purif.
46
56-63
2006
Hordeum vulgare (Q9LLY2), Hordeum vulgare
Manually annotated by BRENDA team
Stanley, D.; Rejzek, M.; Naested, H.; Smedley, M.; Otero, S.; Fahy, B.; Thorpe, F.; Nash, R.J.; Harwood, W.; Svensson, B.; Denyer, K.; Field, R.A.; Smith, A.M.
The role of alpha-glucosidase in germinating barley grains
Plant Physiol.
155
932-943
2011
Hordeum vulgare
Manually annotated by BRENDA team