Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.2.1.21 extracted from

  • 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 (2007), J. Mol. Biol., 371, 1204-1218.
    View publication on PubMed
Search for more literature for 3.2.1.21

Cloned(Commentary)

Cloned (Comment) Organism
expression of isozyme BglB in Escherichia coli Paenibacillus polymyxa

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Paenibacillus polymyxa

Inhibitors

Inhibitors Comment Organism Structure
2-deoxy-2-fluoro-alpha-D-glucopyranose
-
 Paenibacillus polymyxa
thiocellobiose a substrate analogue-type inhibitor, competitive inhibition, binding structure and inhibition mechanism, overview Paenibacillus polymyxa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
100
-
 cellobiose
-
 Paenibacillus polymyxa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
52000
-
 1 * 52000, isozyme BglB, SDS-PAGE Paenibacillus polymyxa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
cellobiose + H2O Paenibacillus polymyxa
-
 2 beta-D-glucose
-
 ?

Organism

Organism UniProt Comment Textmining
Paenibacillus polymyxa P22073 isozymes BglA and BglB
-

Purification (Commentary)

Purification (Comment) Organism
recombinant isozyme BglB from Escherichia coli to homogeneity Paenibacillus polymyxa

Reaction

Reaction Comment Organism Reaction ID
celloheptaose + 6 H2O = 7 beta-D-glucose 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 Paenibacillus polymyxa
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl beta-D-glucopyranoside + H2O
-
 Paenibacillus polymyxa 4-nitrophenol + beta-D-glucose
-
 ?
cellobiose + H2O
-
 Paenibacillus polymyxa 2 beta-D-glucose
-
 ?
cellobiose + H2O BglA is highly specific for cellobiose, BglB acts as an exo-beta-glucosidase hydrolyzing cellobiose and cellodextrins of higher degree of polymerization Paenibacillus polymyxa 2 beta-D-glucose
-
 ?
cellotetraose + 3 H2O substrate binding site and structure, overview Paenibacillus polymyxa 4 beta-D-glucose
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 52000, isozyme BglB, SDS-PAGE Paenibacillus polymyxa
More oligomerization in BglA can assist in fine-tuning the specificity of the active centre by modulating the loops surrounding the cavity, BglB aglycon site structure, overview Paenibacillus polymyxa

Synonyms

Synonyms Comment Organism
beta-glucosidase B
-
 Paenibacillus polymyxa
BglA
-
 Paenibacillus polymyxa
BglB
-
 Paenibacillus polymyxa
More the enzyme belongs to the glycosyl hydrolase family 1 Paenibacillus polymyxa

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
21
-
 thiocellobiose
-
 Paenibacillus polymyxa

pI Value

Organism Comment pI Value Maximum pI Value
Paenibacillus polymyxa about, isozyme BglB, isoelectric focusing
-
 5