Cloned (Comment) | Organism |
---|---|
gene nit, the gene is encoded in the nic-gene cluster located on plasmid pAO1 and flanked by mobile elements | Paenarthrobacter nicotinovorans |
the gene is encoded in the nic-gene cluster on the chromosome | Rhodococcus opacus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-oxoglutaramate + H2O | Rhodococcus opacus | - |
2-oxoglutarate + NH3 | - |
? | |
2-oxoglutaramate + H2O | Nocardioides sp. | - |
2-oxoglutarate + NH3 | - |
? | |
2-oxoglutaramate + H2O | Paenarthrobacter nicotinovorans | - |
2-oxoglutarate + NH3 | - |
? | |
2-oxoglutaramate + H2O | Nocardioides sp. JS614 / ATCC BAA-499 | - |
2-oxoglutarate + NH3 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Nocardioides sp. | - |
- |
- |
Nocardioides sp. JS614 / ATCC BAA-499 | - |
- |
- |
Paenarthrobacter nicotinovorans | - |
gene nit | - |
Rhodococcus opacus | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-oxoglutaramate + H2O | - |
Rhodococcus opacus | 2-oxoglutarate + NH3 | - |
? | |
2-oxoglutaramate + H2O | - |
Nocardioides sp. | 2-oxoglutarate + NH3 | - |
? | |
2-oxoglutaramate + H2O | - |
Paenarthrobacter nicotinovorans | 2-oxoglutarate + NH3 | - |
? | |
2-oxoglutaramate + H2O | the conserved Cys-Glu-Lys triad is involved in catalysis | Paenarthrobacter nicotinovorans | 2-oxoglutarate + NH3 | - |
? | |
2-oxoglutaramate + H2O | - |
Nocardioides sp. JS614 / ATCC BAA-499 | 2-oxoglutarate + NH3 | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Rhodococcus opacus |
30 | - |
assay at | Nocardioides sp. |
30 | - |
assay at | Paenarthrobacter nicotinovorans |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.1 | - |
assay at | Rhodococcus opacus |
7.1 | - |
assay at | Nocardioides sp. |
7.1 | - |
assay at | Paenarthrobacter nicotinovorans |
General Information | Comment | Organism |
---|---|---|
metabolism | the omega-amidase is involved in the nicotine catabolism, and encoded in organized clusters of homologous genes for nicotine catabolism. The omega-amidase, together with glutamate dehydrogenase, may form a physiologically relevant enzyme couple, leading to transformation of metabolically inert alpha-oxoglutaramate derived from trihydroxypyridine into glutamate, a central compound of nitrogen metabolism | Rhodococcus opacus |
metabolism | the omega-amidase is involved in the nicotine catabolism, and encoded in organized clusters of homologous genes for nicotine catabolism. The omega-amidase, together with glutamate dehydrogenase, may form a physiologically relevant enzyme couple, leading to transformation of metabolically inert alpha-oxoglutaramate derived from trihydroxypyridine into glutamate, a central compound of nitrogen metabolism | Nocardioides sp. |
metabolism | the omega-amidase is involved in the nicotine catabolism, and encoded in organized clusters of homologous genes for nicotine catabolism. The omega-amidase, together with glutamate dehydrogenase, may form a physiologically relevant enzyme couple, leading to transformation of metabolically inert alpha-oxoglutaramate derived from trihydroxypyridine into glutamate, a central compound of nitrogen metabolism | Paenarthrobacter nicotinovorans |
physiological function | the omega-amidase, together with glutamate dehydrogenase, may form a physiologically relevant enzyme couple, leading to transformation of metabolically inert alpha-oxoglutaramate derived from trihydroxypyridine into glutamate, a central compound of nitrogen metabolism | Rhodococcus opacus |
physiological function | the omega-amidase, together with glutamate dehydrogenase, may form a physiologically relevant enzyme couple, leading to transformation of metabolically inert alpha-oxoglutaramate derived from trihydroxypyridine into glutamate, a central compound of nitrogen metabolism | Nocardioides sp. |
physiological function | the omega-amidase, together with glutamate dehydrogenase, may form a physiologically relevant enzyme couple, leading to transformation of metabolically inert alpha-oxoglutaramate derived from trihydroxypyridine into glutamate, a central compound of nitrogen metabolism | Paenarthrobacter nicotinovorans |