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Information on EC 3.2.1.86 - 6-phospho-beta-glucosidase and Organism(s) Escherichia coli and UniProt Accession Q46829

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IUBMB Comments
Also hydrolyses several other phospho-beta-D-glucosides, but not their non-phosphorylated forms.
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This record set is specific for:
Escherichia coli
UNIPROT: Q46829
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
phospho-beta-glucosidase, 6-phospho-alpha-glucosidase, phospho-alpha-glucosidase, 6-phospho-beta-glucosidase, gan1d, lacg2, spy1599, lacg1, bgla-2, bgl-2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho-beta-glucosidase A
-
Cellobiose-6-phosphate hydrolase
-
-
-
-
phospho-beta-glucosidase
-
-
-
-
phospho-beta-glucosidase A
-
-
-
-
phosphocellobiase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
6-phospho-beta-D-glucosyl-(1->4)-D-glucose glucohydrolase
Also hydrolyses several other phospho-beta-D-glucosides, but not their non-phosphorylated forms.
CAS REGISTRY NUMBER
COMMENTARY hide
37205-51-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
6-phospho-beta-D-glucosyl-(1->4)-D-glucose + H2O
D-glucose + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
arbutin + H2O
?
show the reaction diagram
-
-
-
?
esculin + H2O
?
show the reaction diagram
-
-
-
?
salicin + H2O
?
show the reaction diagram
-
-
-
?
2-nitrophenyl beta-D-galactoside 6-phosphate + H2O
2-nitrophenol + beta-D-galactose 6-phosphate
show the reaction diagram
-
-
-
-
?
4-methyl-2-oxo-2H-chromen-7-yl 6-O-phosphono-beta-D-glucopyranoside + H2O
?
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside 6-phosphate + H2O
4-nitrophenol + beta-D-glucopyranose 6-phosphate
show the reaction diagram
-
-
-
?
4-nitrothiophenyl beta-D-glucoside 6-phosphate + H2O
4-nitrothiophenol + beta-D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
arbutin 6-phosphate + H2O
hydroquinone + D-glucose 6-phosphate
show the reaction diagram
cellobiose 6-phosphate + H2O
D-glucose 6-phosphate + D-glucose
show the reaction diagram
-
-
-
?
gentiobiose 6-phosphate + H2O
D-glucose 6-phosphate + D-glucose
show the reaction diagram
-
-
-
?
methyl beta-glucoside 6-phosphate + H2O
?
show the reaction diagram
o-nitrophenyl-beta-D-galactopyranoside 6-phosphate + H2O
o-nitrophenol + D-galactose 6-phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside 6-phosphate + H2O
p-nitrophenol + D-glucopyranose 6-phosphate
show the reaction diagram
p-nitrothiophenyl beta-glucoside 6-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
phenyl beta-D-glucoside 6-phosphate + H2O
phenol + glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
salicin 6-phosphate + H2O
2-hydroxymethylphenol + D-glucose 6-phosphate
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
6-phospho-beta-D-glucosyl-(1->4)-D-glucose + H2O
D-glucose + D-glucose 6-phosphate
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3',5'-AMP
-
-
DL-alpha-glycerol-phosphate
-
-
fructose-1,6-diphosphate
-
-
phosphoenolpyruvate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.25
2-nitrophenyl beta-D-galactoside 6-phosphate
-
isoenzyme B
-
0.3
4-methyl-2-oxo-2H-chromen-7-yl 6-O-phosphono-beta-D-glucopyranoside
-
0.44
4-nitrophenyl beta-D-glucopyranoside 6-phosphate
-
0.11
4-nitrothiophenyl beta-D-glucoside 6-phosphate
-
isoenzyme B
-
12.5
6-O-(6-O-phosphono-beta-D-glucopyranosyl)-beta-D-glucopyranose
-
0.35
arbutin 6-phosphate
-
1.3
cellobiose 6-phosphate
-
0.19 - 2.22
methyl beta-D-glucoside 6-phosphate
0.18
p-nitrophenyl-beta-D-glucopyranoside 6-phosphate
-
isoenzyme B
0.33
p-nitrophenyl-D-beta-D-glucopyranoside 6-phosphate
-
isoenzyme A
0.46 - 0.6
phenyl beta-D-glucoside 6-phosphate
0.44 - 0.51
Salicin 6-phosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3
-
isoenzyme A, p-nitrophenyl beta-D-glucospyranoside
7 - 9
-
isoenzyme B, p-nitrophenyl beta-D-glucospyranoside
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
132000
-
isoenzyme B, molecular sieve chromatography together with sedimentation velocity measurement
142000
-
isoenzyme A, molecular sieve chromatography together with sedimentation velocity measurement
21000
gel filtration
50000
SDS-PAGE
65000
-
isoenzyme B, SDS-PAGE
68000
-
isoenzyme A, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
homodimer, 2 * 68000 isoenzyme A, 2 * 65000 isoenzyme B, SDS-PAGE
tetramer
4 * 50000
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C195G
the mutant shows significantly enhanced activity towards salicin compared to the wild type enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 10
-
for more than 1 h
136924
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 28
-
isoenzyme B
25 - 45
-
isoenzyme A
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
isoenzyme A, 4°C, 1 year, sterile starting buffer, 0% loss in activity
-
isoenzyme B, -20°C, 2 months, sterile starting buffer, 50% loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schnetz, K.; Toloczyki, C.; Rak, B.
beta-Glucoside (bgl) operon of Escherichia coli K-12: nucleotide sequence, genetic organization, and possible evolutionary relationship to regulatory components of two Bacillus subtilis genes
J. Bacteriol.
169
2579-2590
1987
Escherichia coli
Manually annotated by BRENDA team
Wilson, G.; Fox, C.F.
The beta-glucoside system of Escherichia coli. IV. Purification and properties of phospho-beta-glucosidases A and B
J. Biol. Chem.
249
5586-5598
1974
Escherichia coli
Manually annotated by BRENDA team
Prasad, I.; Young, B.; Schaefler, S.
Genetic determination of the constitutive biosynthesis of phospho-beta-glucosidase A in Escherichia coli K-12
J. Bacteriol.
114
909-915
1973
Escherichia coli
Manually annotated by BRENDA team
Thompson, J.; Ruvinov, S.B.; Freedberg, D.I.; Hall, B.G.
Cellobiose-6-phosphate hydrolase (CelF) of Escherichia coli: Characterization and Assignment to the unsual family 4 of glycosylhydrolases
J. Bacteriol.
181
7339-7345
1999
Escherichia coli (P17411), Escherichia coli
Manually annotated by BRENDA team
Zangoui, P.; Vashishtha, K.; Mahadevan, S.
Evolution of aromatic beta-glucoside utilization by successive mutational steps in Escherichia coli
J. Bacteriol.
197
710-716
2015
Escherichia coli (Q46829)
Manually annotated by BRENDA team