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Information on EC 3.2.1.20 - alpha-glucosidase and Organism(s) Erwinia rhapontici and UniProt Accession Q9AI65

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:
Erwinia rhapontici
UNIPROT: Q9AI65
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The taxonomic range for the selected organisms is: Erwinia rhapontici
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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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
6-phospho-alpha-glucosidase
-
phospho-alpha-glucosidase
-
acid maltase
-
-
-
-
AGL
-
-
-
-
alpha-1,4-glucosidase
-
-
-
-
alpha-D-glucosidase
-
-
-
-
alpha-glucopyranosidase
-
-
-
-
alpha-glucosid-specific GH4 enzyme
-
-
alpha-glucosidase
alpha-glucoside hydrolase
-
-
-
-
glucoinvertase
-
-
-
-
glucosidoinvertase
-
-
-
-
glucosidosucrase
-
-
-
-
maltase
-
-
-
-
maltase-glucoamylase
-
-
-
-
additional information
the enzyme belongs to the glycsoylhydrolase family GH4. Glycosyl hydrolase family 4, GH4 is exceptional among the 114 families in this enzyme superfamily. Members of GH4 exhibit unusual cofactor requirements for activity, and an essential cysteine residue is present at the active site
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
1-O-alpha-D-glucopyranosyl-beta-D-fructofuranoside + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
-
-
-
?
3-O-alpha-D-glucopyranosyl-D-fructose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
show the reaction diagram
assay at pH 7.5, 37°
-
-
?
4-O-alpha-D-glucopyranosyl-D-fructose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
-
-
-
?
4-O-alpha-D-glucopyranosyl-D-glucopyranose + H2O
alpha-D-glucose + alpha-D-glucose
show the reaction diagram
-
-
-
?
4-O-alpha-D-glucopyranosyl-D-sorbitol + H2O
alpha-D-glucose + D-sorbitol
show the reaction diagram
-
-
-
?
5-O-alpha-D-glucopyranosyl-D-fructose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
-
-
-
?
6-O-alpha-D-glucopyranosyl-D-fructofuranoside + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
22.11
1-O-alpha-D-glucopyranosyl-beta-D-fructofuranoside
-
10.04
3-O-alpha-D-glucopyranosyl-D-fructose
-
1.75
4-O-alpha-D-glucopyranosyl-D-fructose
-
8.58
4-O-alpha-D-glucopyranosyl-D-glucopyranose
-
7.31
4-O-alpha-D-glucopyranosyl-D-sorbitol
-
5.31
5-O-alpha-D-glucopyranosyl-D-fructose
-
2.52
6-O-alpha-D-glucopyranosyl-D-fructofuranoside
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.27
1-O-alpha-D-glucopyranosyl-beta-D-fructofuranoside
-
0.38
3-O-alpha-D-glucopyranosyl-D-fructose
-
0.45
4-O-alpha-D-glucopyranosyl-D-fructose
-
0.85
4-O-alpha-D-glucopyranosyl-D-glucopyranose
-
0.2
4-O-alpha-D-glucopyranosyl-D-sorbitol
-
0.37
5-O-alpha-D-glucopyranosyl-D-fructose
-
0.58
6-O-alpha-D-glucopyranosyl-D-fructofuranoside
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain DSM448, gene palH
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PALH_ERWRD
453
0
50341
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E173S
site-directed mutagenesis
E173S/I174V
site-directed mutagenesis
I174V
site-directed mutagenesis
E173S
mutation with loss of al alpha-glucosidase activity, but the mutant protein exhibits no alpha-galactosidase activtiy
E173S/I174V
mutation with loss of al alpha-glucosidase activity, but the mutant protein exhibits no alpha-galactosidase activtiy
I174V
mutation with loss of al alpha-glucosidase activity, but the mutant protein exhibits no alpha-galactosidase activtiy
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant soluble His-tagged wild-type and mutant PalHs from Escherichia coli by ultracentrifugation, anion exchange chromatography, and gel filtration
anion exchange chormatography and gel filtration chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene palH, palH is present in a cluster of nine genes whose products may facilitate the transport, and metabolism of palatinose in this plant pathogen, phylogenetic analysis, expression of soluble His-tagged wild-type and mutant PalHs in Escherichia coli
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hall, B.G.; Pikis, A.; Thompson, J.
Evolution and biochemistry of family 4 glycosidases: implications for assigning enzyme function in sequence annotations
Mol. Biol. Evol.
26
2487-2497
2009
Erwinia rhapontici, Erwinia rhapontici (Q9AI65), Erwinia rhapontici DSM 448 (Q9AI65)
Manually annotated by BRENDA team