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Information on EC 3.2.1.21 - beta-glucosidase and Organism(s) Paenibacillus polymyxa and UniProt Accession P22073

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EC Tree
IUBMB Comments
Wide specificity for beta-D-glucosides. Some examples also hydrolyse one or more of the following: beta-D-galactosides, alpha-L-arabinosides, beta-D-xylosides, beta-D-fucosides.
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This record set is specific for:
Paenibacillus polymyxa
UNIPROT: P22073
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The taxonomic range for the selected organisms is: Paenibacillus polymyxa
The enzyme appears in selected viruses and cellular organisms
Synonyms
beta-glucosidase, linamarase, beta-glu, emulsin, bglu1, zm-p60.1, bgl1b, cel3a, novozyme 188, t-cell inhibitor, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-glucosidase B
-
amygdalase
-
-
-
-
amygdalinase
-
-
-
-
arbutinase
-
-
-
-
aryl-beta-glucosidase
-
-
-
-
beta-1,6-glucosidase
-
-
-
-
beta-D-glucosidase
-
-
-
-
beta-D-glucoside glucohydrolase
-
-
-
-
beta-glucoside hydrolase
-
-
-
-
BGA
-
-
-
-
cellobiase
-
-
-
-
elaterase
-
-
-
-
emulsin
-
-
-
-
gentiobiase
-
-
-
-
limarase
-
-
-
-
Novozyme 188
-
-
-
-
p-nitrophenyl beta-glucosidase
-
-
-
-
primeverosidase
-
-
-
-
salicilinase
-
-
-
-
T-cell inhibitor
-
-
-
-
vicianase
-
-
-
-
additional information
the enzyme belongs to the glycosyl hydrolase family 1
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose
show the reaction diagram
molecular basis of the catalytic mechanism involving the acid/base Glu167 and the nucleophilic Glu356, the structure of BglB shows that several polar residues narrow the active site pocket and contour additional subsites, detailed substrate-binding mode and oligosaccharide-enzyme recognition pattern of BglB, overview, oligomerization in BglA can assist in fine-tuning the specificity of the active centre by modulating the loops surrounding the cavity
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
beta-D-glucoside glucohydrolase
Wide specificity for beta-D-glucosides. Some examples also hydrolyse one or more of the following: beta-D-galactosides, alpha-L-arabinosides, beta-D-xylosides, beta-D-fucosides.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-22-3
-
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 beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
-
-
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
show the reaction diagram
cellobiose + H2O
2 beta-D-glucose
show the reaction diagram
cellotetraose + 3 H2O
4 beta-D-glucose
show the reaction diagram
substrate binding site and structure, overview
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
show the reaction diagram
-
-
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
show the reaction diagram
-
cellobiose
additional product: cellotriose by transglycosylation activity
r
cellobiose + H2O
2 beta-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
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
show the reaction diagram
cellobiose + H2O
2 beta-D-glucose
show the reaction diagram
-
-
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
show the reaction diagram
-
cellobiose
additional product: cellotriose by transglycosylation activity
r
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-deoxy-2-fluoro-alpha-D-glucopyranose
-
thiocellobiose
a substrate analogue-type inhibitor, competitive inhibition, binding structure and inhibition mechanism, overview
beta-D-glucose
-
competitive inhibition, Ki: 19 mM
DTT
-
30% inhibition at 5 mM
Hg2+
-
strong inhibition at 1 mM
SDS
-
85% inhibition at 5 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6
4-nitrophenyl-beta-D-glucopyranoside
-
-
13
cellobiose
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
21
thiocellobiose
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
about, isozyme BglB, isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
genomic library
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BGLA_PAEPO
448
0
51649
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52000
1 * 52000, isozyme BglB, SDS-PAGE
50000
-
SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 52000, isozyme BglB, SDS-PAGE
octamer
composed of 8 identical subunits, (alpha/beta)-8-barrel-structural fold, crystal structure analysis
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2.4 and 2.3 A resolution, complexed with gluconate ligand
isozyme BglB with bound inhibitors 2-deoxy-2-fluoro-alpha-D-glucopyranose or thiocellobiose, glucose, or as BglB-cellotetraose complex, X-ray difraction structure determination and analysis at 2.15-2.45 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant isozyme BglB from Escherichia coli to homogeneity
to homogeneity, recombinant enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of isozyme BglB in Escherichia coli
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sanz-Aparicio, J.; Hermoso, J.A.; Martinez-Ripoll, M.; Lequerica, J.L.; Polaina, J.
Crystal structure of beta-glucosidase A from Bacillus polymyxa: insights into the catalytic activity in family 1 glycosyl hydrolases
J. Mol. Biol.
275
491-502
1998
Paenibacillus polymyxa (P22073), Paenibacillus polymyxa
Manually annotated by BRENDA team
Painbeni, E.; Valles, S.; Polaina, J.; Flors, A.
Purification and characterization of a Bacillus polymyxa beta-glucosidase expressed in Escherichia coli
J. Bacteriol.
174
3087-3091
1992
Paenibacillus polymyxa
Manually annotated by BRENDA team
Isorna, P.; Polaina, J.; Latorre-Garcia, L.; Canada, F.J.; Gonzalez, B.; Sanz-Aparicio, J.
Crystal structures of Paenibacillus polymyxa beta-glucosidase B complexes reveal the molecular basis of substrate specificity and give new insights into the catalytic machinery of family I glycosidases
J. Mol. Biol.
371
1204-1218
2007
Paenibacillus polymyxa (P22073), Paenibacillus polymyxa
Manually annotated by BRENDA team