Any feedback?
Literature summary for 3.5.1.49 extracted from
- Biochemical and mutational studies of the Bacillus cereus CECT 5050T formamidase support the existence of a C-E-E-K tetrad in several members of the nitrilase superfamily (2011), Appl. Environ. Microbiol., 77, 5761-5769.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli BL21(DE3) cells | Bacillus cereus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E140D | the mutation does not significantly alter enzyme folding and shows no detectable activity | Bacillus cereus |
| W136H | this mutation causes the absence of overexpression of the enzyme | Bacillus cereus |
| Y191F | the mutation does not significantly alter enzyme folding and shows 11.8% activity compared to the wild type enzyme | Bacillus cereus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Hg2+ | complete inhibition at concentrations above 15 mM | Bacillus cereus |  |
| iodoacetamide | complete inhibition at concentrations above 15 mM | Bacillus cereus | |
| additional information | the presence of EDTA and dithiothreitol has no significant effect on enzyme activity | Bacillus cereus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 108 | - |
Formamide | in 100 mM sodium citrate buffer (pH 6.0), at 50°C | Bacillus cereus | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | the presence of K+, Na+, Ca2+, Mg2+, and Pb2+ has no significant effect on enzyme activity | Bacillus cereus |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 38000 | - |
4 * 38000, His-tagged enzyme, SDS-PAGE | Bacillus cereus |
| 38632 | - |
4 * 38632, His-tagged enzyme, calculated from amino acid sequence | Bacillus cereus |
| 135000 | 160000 | gel filtration | Bacillus cereus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetamide + H2O | Bacillus cereus | - |
acetate + NH3 | - |
? | |
| acetamide + H2O | Bacillus cereus CECT 5050T | - |
acetate + NH3 | - |
? | |
| formamide + H2O | Bacillus cereus | best substrate | formate + NH3 | - |
? | |
| formamide + H2O | Bacillus cereus CECT 5050T | best substrate | formate + NH3 | - |
? | |
| additional information | Bacillus cereus | propionamide, butyramide, isobutyramide, alaninamide, leucinamide, glycinamide, and urea are not recognized as substrates | ? | - |
? | |
| additional information | Bacillus cereus CECT 5050T | propionamide, butyramide, isobutyramide, alaninamide, leucinamide, glycinamide, and urea are not recognized as substrates | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus cereus | - |
- |
- |
| Bacillus cereus CECT 5050T | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| Talon metal-affinity resin column chromatography and Superdex 200 gel filtration | Bacillus cereus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetamide + H2O | - |
Bacillus cereus | acetate + NH3 | - |
? | |
| acetamide + H2O | - |
Bacillus cereus CECT 5050T | acetate + NH3 | - |
? | |
| formamide + H2O | best substrate | Bacillus cereus | formate + NH3 | - |
? | |
| formamide + H2O | best substrate | Bacillus cereus CECT 5050T | formate + NH3 | - |
? | |
| additional information | propionamide, butyramide, isobutyramide, alaninamide, leucinamide, glycinamide, and urea are not recognized as substrates | Bacillus cereus | ? | - |
? | |
| additional information | propionamide, butyramide, isobutyramide, alaninamide, leucinamide, glycinamide, and urea are not recognized as substrates | Bacillus cereus CECT 5050T | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homotetramer | 4 * 38000, His-tagged enzyme, SDS-PAGE | Bacillus cereus |
| homotetramer | 4 * 38632, His-tagged enzyme, calculated from amino acid sequence | Bacillus cereus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AmiF | - |
Bacillus cereus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
- |
Bacillus cereus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 35 | 70 | about 50% activity at 35 and 70°C | Bacillus cereus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | 75 | after incubation at the optimal temperature for activity of the enzyme (50°C) for 40 h, the enzyme maintains around 95% of its initial activity. Activity is gradually lost when the enzyme is incubated at temperatures over 65°C for 30 min. The melting temperature is at 73.5°C | Bacillus cereus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
maximum activity in citrate and cacodylate buffers at pH 6.0. Using sodium phosphate as the buffering agent as opposed to cacodylate/citrate, a decrease in enzyme activity is observed at pH 6.0 | Bacillus cereus |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
