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Information on EC 3.2.1.20 - alpha-glucosidase and Organism(s) Picrophilus torridus and UniProt Accession Q6L2X4

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:
Picrophilus torridus
UNIPROT: Q6L2X4
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Word Map
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The taxonomic range for the selected organisms is: Picrophilus torridus
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
-
-
-
-
maltase
-
-
-
-
maltase-glucoamylase
-
-
-
-
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
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
show the reaction diagram
low activity
-
-
?
dextrin 10 + H2O
alpha-D-glucose
show the reaction diagram
27% of the activity with maltose
-
-
?
maltohexaose + H2O
maltopentaose + D-glucose
show the reaction diagram
-
-
-
?
maltopentaose + H2O
alpha-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
54% of the activity with maltose
-
-
?
maltotriose + H2O
maltose + alpha-D-glucose
show the reaction diagram
-
-
-
?
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 + D-glucose
show the reaction diagram
probable physiological role of the enzyme in the utilization of exogenous glycoproteins and/or in the turnover of the organism’s own glycoproteins, overview
-
-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
87
recombinant AglA
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain DSM 9790, gene aglA
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
440000
recombinant AglA, gel filtration
72000
6 * 72000, recombinant AglA, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
6 * 72000, recombinant AglA, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
15 min, inactivation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant AglA 39.3fold from Escherichia coli strain BL21 by heat treatment for 15 min at 67°C, hydrophobic interaction and anion exchange chromatography, and gel filtration in presence of 150 mM NaCl
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene aglA, expression analysis and mapping of transcription start sites, the gene is clustered in the genome and shows colinear orientation and a small intergenic space with gene manA encoding alpha-mannosidase, the genes are independently transcribed, both producing leaderless mRNA, phylogenetic tree, overexpression in Escherichia coli strain BL21, subcloning in Escherichia coli strain XL-1 Blue
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Angelov, A.; Putyrski, M.; Liebl, W.
Molecular and biochemical characterization of alpha-glucosidase and alpha-mannosidase and their clustered genes from the thermoacidophilic archaeon Picrophilus torridus
J. Bacteriol.
188
7123-7131
2006
Picrophilus torridus (Q6L2X4), Picrophilus torridus
Manually annotated by BRENDA team