Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-(R)-hydroxypropyl-CoM + NAD+ | Xanthobacter autotrophicus | - |
2-oxopropyl-CoM + NADH + H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Xanthobacter autotrophicus | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-(R)-hydroxypropyl-CoM + NAD+ | - |
Xanthobacter autotrophicus | 2-oxopropyl-CoM + NADH + H+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
(R)-hydroxypropyl-coenzyme M dehydrogenase | - |
Xanthobacter autotrophicus |
R-HPCDH | - |
Xanthobacter autotrophicus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Xanthobacter autotrophicus |
General Information | Comment | Organism |
---|---|---|
metabolism | the bacterium produces R- and S-HPCDH, EC 1.1.1.268 and EC 1.1.1.269, simultaneously to facilitate transformation of R- and S-enantiomers of epoxy-propane to a common achiral product 2-ketopropyl-CoM | Xanthobacter autotrophicus |
additional information | structural basis for stereospecificity of R-HPCDH, comparison to S-HPCDH, EC 1.1.1.269, overview. Placement of catalytic residues within the active site of each enzyme is nearly identical, structural differences in the surrounding area provide each enzyme with a distinct substrate binding pocket | Xanthobacter autotrophicus |