Crystallization (Comment) | Organism |
---|---|
purified recombinant enzyme, X-ray diffraction structure determination and analysis | Xanthobacter autotrophicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(2S)-2-hydroxypropyl-CoM + NAD+ | Xanthobacter autotrophicus | - |
2-oxopropyl-CoM + NADH + H+ | - |
r | |
(2S)-2-hydroxypropyl-CoM + NAD+ | Xanthobacter autotrophicus ATCC BAA-1158 | - |
2-oxopropyl-CoM + NADH + H+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Xanthobacter autotrophicus | Q56841 | - |
- |
Xanthobacter autotrophicus ATCC BAA-1158 | Q56841 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
(2S)-2-hydroxypropyl-CoM + NAD+ = 2-oxopropyl-CoM + NADH + H+ | active site structure modeling and stereochemistry of reaction mechanism, overview | Xanthobacter autotrophicus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(2S)-2-hydroxypropyl-CoM + NAD+ | - |
Xanthobacter autotrophicus | 2-oxopropyl-CoM + NADH + H+ | - |
r | |
(2S)-2-hydroxypropyl-CoM + NAD+ | substrate binding structure, overview | Xanthobacter autotrophicus | 2-oxopropyl-CoM + NADH + H+ | - |
r | |
(2S)-2-hydroxypropyl-CoM + NAD+ | - |
Xanthobacter autotrophicus ATCC BAA-1158 | 2-oxopropyl-CoM + NADH + H+ | - |
r | |
(2S)-2-hydroxypropyl-CoM + NAD+ | substrate binding structure, overview | Xanthobacter autotrophicus ATCC BAA-1158 | 2-oxopropyl-CoM + NADH + H+ | - |
r | |
additional information | substrate specificity of the stereochemically different isozymes, R-HPCDH (EC 1.1.1.268) and S-HPCDH are 41% identical to each other, overview | Xanthobacter autotrophicus | ? | - |
- |
|
additional information | substrate specificity of the stereochemically different isozymes, R-HPCDH (EC 1.1.1.268) and S-HPCDH are 41% identical to each other, overview | Xanthobacter autotrophicus ATCC BAA-1158 | ? | - |
- |
Synonyms | Comment | Organism |
---|---|---|
(S)-hydroxypropyl-coenzyme M dehydrogenase | - |
Xanthobacter autotrophicus |
S-HPCDH | - |
Xanthobacter autotrophicus |
xecE | - |
Xanthobacter autotrophicus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Xanthobacter autotrophicus | |
NADH | - |
Xanthobacter autotrophicus |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the short-chain dehydrogenases/reductase (SDR) superfamily of enzymes. The C-terminal domains of SDR enzymes are responsible for imparting substrate specificity | Xanthobacter autotrophicus |
metabolism | (R)- and (S)-hydroxypropyl-coenzyme M dehydrogenase (R- and S-HPCDH), are part of a bacterial pathway of short-chain alkene and epoxide metabolism. R- and S-HPCDH act on different substrate enantiomers in a common pathway | Xanthobacter autotrophicus |
additional information | structure-function relationship, active site structure modeling and stereochemistry of reaction mechanism, overview. The C-terminal domains of SDR enzymes are responsible for imparting substrate specificity | Xanthobacter autotrophicus |