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Information on EC 3.2.1.20 - alpha-glucosidase and Organism(s) Thermotoga maritima and UniProt Accession O33830

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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:
Thermotoga maritima
UNIPROT: O33830
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Word Map
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The taxonomic range for the selected organisms is: Thermotoga maritima
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
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-methylumbelliferyl alpha-D-galactopyranoside + H2O
4-methylumbelliferone + alpha-D-galactopyranose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl alpha-D-glucopyranoside + H2O
4-methylumbelliferone + alpha-D-glucopyranose
show the reaction diagram
-
-
-
?
4-nitrophenyl alpha-D-galactopyranoside + H2O
4-nitrophenol + alpha-D-galactopyranose
show the reaction diagram
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
show the reaction diagram
-
-
-
?
n-dodecyl-beta-D-maltoside + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
activates, can partially substitute for Mn2+
Mn2+
activates, dependent on, 1 mM required
Ni2+
activates, can partially substitute for Mn2+
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
complete inhibition at 2 mM
Hg2+
98% inhibition at 0.1 mM, due to existence of essential sulfhydryl groups in the enzyme
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
slight activation, 600 mM are required for maximal activity, cannot substitute for DTT
DTT
dependent on reducing agents, 50 mM or more required for maximal activity, due to existence of essential sulfhydryl groups in the enzyme
L-cysteine
can only partially substitute for DTT with 3fold less activation at 60 mM
NAD+
dependent on, 0.9 mM required
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.53
4-nitrophenyl alpha-D-galactopyranoside
pH 7.0, 60°C
0.23
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 60°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10.48
4-nitrophenyl alpha-D-galactopyranoside
pH 7.0, 60°C
9.12
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 60°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
50% of maximal activity at pH 6.5 and pH 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65 - 100
50% of maximal activity at 65°C and 100°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme AglA, gene aglA
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110000
gel filtration
58000
2 * 58000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 58000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
loss of 50% activity in 48 h
70
loss of 80% activity in 48 h
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli, by heat denaturation and ion exchange chromatography, large scale, to near homogeneity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, genomic organization of the gene cluster, functional overexpression in Escherichia coli JM83
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Raasch, C.; Streit, W.; Schanzer, J.; Bibel, M.; Gosslar, U.; Liebl, W.
Thermotoga maritima AglA, an extremely thermostable NAD+-, Mn2+-, and thiol-dependent alpha-glucosidase
Extremophiles
4
189-200
2000
Thermotoga maritima (O33830), Thermotoga maritima
Manually annotated by BRENDA team