Crystallization (Comment) | Organism |
---|---|
enzyme free or bound to substrate 2-ketopropyl-CoM, X-ray structure determination and analysis at 1.6-3.5 A resolution, multiple isomorphous replacement and anomalous scattering using four weak heavy atom derivatives | Xanthobacter autotrophicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH | Xanthobacter autotrophicus | terminal enzyme in the metabolic pathway converting propylene to acetoacetate | 2-mercaptoethanesulfonate + acetoacetate + NADP+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Xanthobacter autotrophicus | Q56839 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
2-mercaptoethanesulfonate + acetoacetate + NADP+ = 2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+ | detailed reaction mechanism in a catalytic cycle, active site structure | Xanthobacter autotrophicus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH | terminal enzyme in the metabolic pathway converting propylene to acetoacetate | Xanthobacter autotrophicus | 2-mercaptoethanesulfonate + acetoacetate + NADP+ | - |
r | |
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH | i.e. 2-ketopropyl-CoM, comparison of enzyme structure with and without bound substrate, binding of 2-ketopropyl-coenzyme M induces a conformational change resulting in collapse of the substrate access channel, substrate binding site structure analysis | Xanthobacter autotrophicus | 2-mercaptoethanesulfonate + acetoacetate + NADP+ | - |
r |
Subunits | Comment | Organism |
---|---|---|
dimer | crystal structure | Xanthobacter autotrophicus |
Synonyms | Comment | Organism |
---|---|---|
2-ketopropyl-coenzyme M oxidoreductase/carboxylase | - |
Xanthobacter autotrophicus |
2-KPCC | - |
Xanthobacter autotrophicus |
More | enzyme belongs to the disulfide oxidoreductase family of enzymes DSOR | Xanthobacter autotrophicus |
NADPH:2-ketopropyl-CoM oxidoreductase/carboxylase | - |
Xanthobacter autotrophicus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | binding domain structure analysis | Xanthobacter autotrophicus | |
NADP+ | binding domain structure analysis | Xanthobacter autotrophicus | |
NADPH | binding domain structure analysis | Xanthobacter autotrophicus |