Cloned (Comment) | Organism |
---|---|
expression of isozyme BglB in Escherichia coli | Paenibacillus polymyxa |
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 | 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 Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
100 | - |
cellobiose | - |
Paenibacillus polymyxa |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
52000 | - |
1 * 52000, isozyme BglB, SDS-PAGE | Paenibacillus polymyxa |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
cellobiose + H2O | Paenibacillus polymyxa | - |
2 beta-D-glucose | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Paenibacillus polymyxa | P22073 | isozymes BglA and BglB | - |
Purification (Comment) | Organism |
---|---|
recombinant isozyme BglB from Escherichia coli to homogeneity | Paenibacillus polymyxa |
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 |
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 | 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 | 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 maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
21 | - |
thiocellobiose | - |
Paenibacillus polymyxa |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Paenibacillus polymyxa | about, isozyme BglB, isoelectric focusing | - |
5 |