EC Number   |
Title |
Organism |
|---|
   1.8.1.5 | Substitution of a conserved catalytic dyad into 2-KPCC causes loss of carboxylation activity |
Xanthobacter autotrophicus |
| 1.8.1.5 | The reactive form of a C-S bond-cleaving, CO2-fixing flavoenzyme |
Xanthobacter autotrophicus |
| 1.8.1.5 | The unique Phe-His dyad of 2-ketopropyl coenzyme M oxidoreductase/carboxylase selectively promotes carboxylation and S-C bond cleavage |
Xanthobacter autotrophicus |
| 1.8.1.5 | A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial pathway of aliphatic epoxide carboxylation |
Xanthobacter sp. |
| 1.8.1.5 | A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial pathway of aliphatic epoxide carboxylation |
Xanthobacter sp. Py2 |
| 1.8.1.5 | Characterization of five catalytic activities associated with the NADPH:2-ketopropyl-coenzyme M [2-(2-ketopropylthio)ethanesulfonate] oxidoreductase/carboxylase of the Xanthobacter strain Py2 epoxide carboxylase system |
Xanthobacter sp. |
| 1.8.1.5 | Characterization of five catalytic activities associated with the NADPH:2-ketopropyl-coenzyme M [2-(2-ketopropylthio)ethanesulfonate] oxidoreductase/carboxylase of the Xanthobacter strain Py2 epoxide carboxylase system |
Xanthobacter sp. Py2 |
| 1.8.1.5 | Crystallization and preliminary X-ray analysis of a NADPH 2-ketopropyl-coenzyme M oxidoreductase/carboxylase |
Xanthobacter sp. |
| 1.8.1.5 | Mechanism of inhibition of aliphatic epoxide carboxylation by the coenzyme M analog 2-bromoethanesulfonate |
Xanthobacter autotrophicus |
| 1.8.1.5 | Mechanistic implications of the structure of the mixed-disulfide intermediate of the disulfide oxidoreductase, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase |
Xanthobacter autotrophicus |
