EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.98.3 | expression in Escherichia coli | Mycobacterium tuberculosis |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.1.98.3 | different crystal forms of ligand-free enzyme reveal considerable levels of structural flexibility of two surface loops that seem to govern accessibility of the active site. Structures of complexes with the benzothiazinone-derived nitroso derivative 3-nitroso-N-[(1R)-1-phenylethyl]-5-(trifluoromethyl)benzamide reveal that inhibitor binding includes a covalent link to conserved Cys387, and reveal a trifluoromethyl group as a second key determinant of interaction with the enzyme. A noncovalent complex is formed between the enzyme and 3-nitro-N-[(1R)-1-phenylethyl]-5-(trifluoromethyl)benzamide, which is structurally identical to 3-nitroso-N-[(1R)-1-phenylethyl]-5-(trifluoromethyl)benzamide except for an inert nitro group replacing the reactive nitroso group. Binding of benzothiazinone-class inhibitors to the enzyme is not strictly dependent on formation of the covalent link to Cys387 | Mycobacterium tuberculosis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.1.98.3 | 3-nitro-N-[(1R)-1-phenylethyl]-5-(trifluoromethyl)benzamide | forms a noncovalent complex with the enzyme | Mycobacterium tuberculosis | |
1.1.98.3 | 3-nitroso-N-[(1R)-1-phenylethyl]-5-(trifluoromethyl)benzamide | benzothiazinone-derived inhibitor, binding includes a covalent link to conserved Cys387, and trifluoromethyl group is a second key determinant of interaction with the enzyme | Mycobacterium tuberculosis |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.98.3 | Mycobacterium tuberculosis | P9WJF1 | - |
- |
1.1.98.3 | Mycobacterium tuberculosis H37Rv | P9WJF1 | - |
- |