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

for references in articles please use BRENDA:EC3.2.1.20
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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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This record set is specific for:
Hordeum vulgare
UNIPROT: Q43763
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The taxonomic range for the selected organisms is: Hordeum vulgare
Reaction Schemes
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, 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
278742
-
maltase
-
-
-
-
maltase-glucoamylase
-
-
-
-
additional information
278742
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
D-glucose
show the reaction diagram
-
-
-
-
?
maltohexaose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
maltopentaose + H2O
alpha-D-glucose
show the reaction diagram
-
-
-
-
?
maltose + H2O
alpha-D-glucose
show the reaction diagram
maltose + H2O
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
?
-
transcription reaches a maximum 48 h after the start of germination
-
-
-
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
alpha-D-glucose
show the reaction diagram
Q9LLY2
-
-
-
?
maltose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
additional information
?
-
Q43763
transcription reaches a maximum 48 h after the start of germination
-
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-deoxynojirimycin
-
-
4-O-alpha-glucosyl-moranoline
-
weak inhibition
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
5.32
isomaltose
-
-
7.89
maltoheptaose
-
-
5.44
maltohexaose
-
-
2.92
maltopentaose
-
-
1.7 - 2.2
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
Q9LLY2
purified recombinant enzyme
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 4.5
-
hydrolysis of maltose, recombinant enzyme
4 - 4.5
hydrolysis of maltose
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
Q9LLY2
assay at
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
AGLU_HORVU
877
0
96933
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
92000
Q9LLY2
wild-type enzyme, gel filtration
100000
Q9LLY2
recombinant enzyme, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Q9LLY2
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
Q9LLY2
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
Q9LLY2
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, Hordeum vulgare (Q43763)
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, Hordeum vulgare (Q9LLY2)
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
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