EC Number | Cloned (Comment) | Organism |
---|---|---|
3.1.1.72 | expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Butyrivibrio proteoclasticus |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.1.1.72 | purified recombinnat wild-type enzyme and mutant H351A, X-ray diffraction structure determination and analysis at 2.1 A and 2.0 A resolution, respectively, single wavelength anomalous diffraction and molecular replacement methods, three-dimensional structure determintaion | Butyrivibrio proteoclasticus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.1.1.72 | H351A | site-directed mutagenesis, inactive mutant | Butyrivibrio proteoclasticus |
3.1.1.72 | S142A | site-directed mutagenesis | Butyrivibrio proteoclasticus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.1.72 | Butyrivibrio proteoclasticus | E0RVY7 | - |
- |
3.1.1.72 | Butyrivibrio proteoclasticus B316 | E0RVY7 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.1.1.72 | recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by metal chelating nickel affinity chromatography | Butyrivibrio proteoclasticus |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.1.72 | 4-nitrophenyl acetate + H2O | - |
Butyrivibrio proteoclasticus | 4-nitrophenol + acetate | - |
? | |
3.1.1.72 | 4-nitrophenyl acetate + H2O | - |
Butyrivibrio proteoclasticus B316 | 4-nitrophenol + acetate | - |
? | |
3.1.1.72 | 4-nitrophenyl butyrate + H2O | - |
Butyrivibrio proteoclasticus | 4-nitrophenol + butyrate | - |
? | |
3.1.1.72 | 4-nitrophenyl butyrate + H2O | - |
Butyrivibrio proteoclasticus B316 | 4-nitrophenol + butyrate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.1.1.72 | More | the enzyme contains a C-terminal SGNH domain and an N-terminal jelly-roll domain typical of CE2 family structures, three-dimensional structure analysis, overview | Butyrivibrio proteoclasticus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.1.72 | acetyl xylan esterase | - |
Butyrivibrio proteoclasticus |
3.1.1.72 | Est2A | - |
Butyrivibrio proteoclasticus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.1.1.72 | 37 | - |
assay at | Butyrivibrio proteoclasticus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.1.1.72 | 7.2 | - |
assay at | Butyrivibrio proteoclasticus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.1.1.72 | evolution | the enzyme belongs to the carbohydrate esterase family 2, CE2, and has a domain structure typical of CE2 family structures, a C-terminal SGNH domain and an N-terminal jelly-roll domain | Butyrivibrio proteoclasticus |
3.1.1.72 | additional information | the active site of the enzyme is located at the base of a groove lined by two tryptophan residues, Trp158 and Trp195 are arranged in a parallel fashion on either side above the active site | Butyrivibrio proteoclasticus |