EC Number | Cloned (Comment) | Organism |
---|---|---|
3.2.1.21 | methanol-inducible expression of wild-type and mutant enzymes in Pichia pastoris strain X-33 | Aspergillus niger |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.2.1.21 | W49A | site-directed mutagenesis, the mutation reduces the transglucosylation activity of the enzyme due to a large decrease in binding capacity for Glc at site +1 and an increase in binding ability at site-1, while the hydrolytic activity is only slightly decreased compared to the wild-type enzyme, the mutant shows altered kinetics, overview | Aspergillus niger |
3.2.1.21 | W49D | site-directed mutagenesis, the mutation reduces the transglucosylation activity of the enzyme due to a large decrease in binding capacity for Glc at site +1 and an increase in binding ability at site-1, while the hydrolytic activity is only slightly decreased compared to the wild-type enzyme, the mutant shows altered kinetics, overview | Aspergillus niger |
3.2.1.21 | W49G | site-directed mutagenesis, the mutation reduces the transglucosylation activity of the enzyme due to a large decrease in binding capacity for Glc at site +1 and an increase in binding ability at site-1, while the hydrolytic activity is only slightly decreased compared to the wild-type enzyme, the mutant shows altered kinetics, overview | Aspergillus niger |
3.2.1.21 | W49N | site-directed mutagenesis, the mutation reduces the transglucosylation activity of the enzyme due to a large decrease in binding capacity for Glc at site +1 and an increase in binding ability at site-1, while the hydrolytic activity is only slightly decreased compared to the wild-type enzyme, the mutant shows altered kinetics, overview | Aspergillus niger |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.2.1.21 | cellobiose | competitive inhibition of wild-type and mutant enzymes | Aspergillus niger | |
3.2.1.21 | D-gluconolactone | competitive inhibition of wild-type enzyme and mutant W49A | Aspergillus niger | |
3.2.1.21 | D-glucose | competitive inhibition of wild-type and mutant enzymes | Aspergillus niger | |
3.2.1.21 | gentiobiose | competitive inhibition of wild-type enzyme and mutant W49A | Aspergillus niger |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.21 | additional information | - |
additional information | kinetics of hydrolytic activity of mutant enzymes and of transglucosylation activities of recombinant wild-type and mutant enzymes, overview | Aspergillus niger | |
3.2.1.21 | 0.27 | - |
cellotetraose | pH 4.5, 25°C, recombinant wild-type enzyme | Aspergillus niger | |
3.2.1.21 | 0.33 | - |
cellopentaose | pH 4.5, 25°C, recombinant wild-type enzyme | Aspergillus niger | |
3.2.1.21 | 0.52 | - |
cellotriose | pH 4.5, 25°C, recombinant wild-type enzyme | Aspergillus niger | |
3.2.1.21 | 1.5 | - |
4-nitrophenyl-beta-D-glucopyranoside | pH 4.5, 25°C, recombinant wild-type enzyme | Aspergillus niger | |
3.2.1.21 | 2.2 | - |
gentiobiose | pH 4.5, 25°C, recombinant wild-type enzyme | Aspergillus niger | |
3.2.1.21 | 2.7 | - |
cellobiose | pH 4.5, 25°C, recombinant wild-type enzyme | Aspergillus niger |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.21 | cellobiose + H2O | Aspergillus niger | - |
2 beta-D-glucose | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.21 | Aspergillus niger | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
3.2.1.21 | celloheptaose + 6 H2O = 7 beta-D-glucose | Trp49 is important for transglucosylation catalytic activity | Aspergillus niger |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.21 | 4-nitrophenyl beta-D-glucopyranoside + H2O | - |
Aspergillus niger | 4-nitrophenol + beta-D-glucose | - |
? | |
3.2.1.21 | cellobiose + H2O | - |
Aspergillus niger | 2 beta-D-glucose | - |
? | |
3.2.1.21 | cellopentaose + H2O | - |
Aspergillus niger | 5 D-glucose | - |
? | |
3.2.1.21 | cellotetraose + 3 H2O | - |
Aspergillus niger | 4 beta-D-glucose | - |
? | |
3.2.1.21 | cellotriose + H2O | - |
Aspergillus niger | 3 D-glucose | - |
? | |
3.2.1.21 | gentiobiose + H2O | - |
Aspergillus niger | 2 beta-D-glucose | - |
? | |
3.2.1.21 | additional information | the enzyme shows transglucosylation activity involving Trp49, overview | Aspergillus niger | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.21 | More | the enzyme belongs to the glycosyl hydrolase family 3 | Aspergillus niger |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.21 | 25 | - |
assay at | Aspergillus niger |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.21 | 2 | 3.7 | cellotriose | pH 4.5, 25°C, recombinant wild-type enzyme | Aspergillus niger | |
3.2.1.21 | 51.7 | - |
cellopentaose | pH 4.5, 25°C, recombinant wild-type enzyme | Aspergillus niger | |
3.2.1.21 | 54.7 | - |
cellotetraose | pH 4.5, 25°C, recombinant wild-type enzyme | Aspergillus niger | |
3.2.1.21 | 70 | - |
gentiobiose | pH 4.5, 25°C, recombinant wild-type enzyme | Aspergillus niger | |
3.2.1.21 | 85.1 | - |
cellotriose | pH 4.5, 25°C, recombinant wild-type enzyme | Aspergillus niger | |
3.2.1.21 | 89 | - |
4-nitrophenyl-beta-D-glucopyranoside | pH 4.5, 25°C, recombinant wild-type enzyme | Aspergillus niger | |
3.2.1.21 | 103 | - |
cellobiose | pH 4.5, 25°C, recombinant wild-type enzyme | Aspergillus niger |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.21 | 4.5 | - |
assay at | Aspergillus niger |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.21 | 0.2 | - |
D-gluconolactone | pH 4.5, 25°C, recombinant mutant W49A | Aspergillus niger | |
3.2.1.21 | 0.4 | - |
D-gluconolactone | pH 4.5, 25°C, recombinant wild-type enzyme | Aspergillus niger | |
3.2.1.21 | 1.1 | - |
cellobiose | pH 4.5, 25°C, recombinant mutant W49D | Aspergillus niger | |
3.2.1.21 | 1.2 | - |
cellobiose | pH 4.5, 25°C, recombinant mutant W49N | Aspergillus niger | |
3.2.1.21 | 1.3 | - |
cellobiose | pH 4.5, 25°C, recombinant mutant W49G | Aspergillus niger | |
3.2.1.21 | 1.4 | - |
cellobiose | pH 4.5, 25°C, recombinant mutant W49A | Aspergillus niger | |
3.2.1.21 | 1.6 | - |
cellobiose | pH 4.5, 25°C, recombinant mutants W49N and W49G | Aspergillus niger | |
3.2.1.21 | 1.8 | - |
gentiobiose | pH 4.5, 25°C, recombinant mutant W49A | Aspergillus niger | |
3.2.1.21 | 1.8 | - |
cellobiose | pH 4.5, 25°C, recombinant wild-type enzyme and mutant W49A | Aspergillus niger | |
3.2.1.21 | 1.9 | - |
cellobiose | pH 4.5, 25°C, recombinant mutant W49D | Aspergillus niger | |
3.2.1.21 | 3 | - |
D-glucose | pH 4.5, 25°C, recombinant wild-type enzyme | Aspergillus niger | |
3.2.1.21 | 4.8 | - |
gentiobiose | pH 4.5, 25°C, recombinant wild-type enzyme | Aspergillus niger |