EC Number   |
General Information |
Reference |
|---|
   1.1.1.269 | 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 |
-, 762714 |
| 1.1.1.269 | 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 |
-, 762714 |
| 1.1.1.269 | 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 acommon achiral product 2-ketopropyl-CoM |
724129 |
| 1.1.1.269 | more |
structural basis for stereospecificity of S-HPCDH, comparison to R-HPCDH, EC 1.1.1.268, 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. The active site of S-HPCDH is located in a cleft between the N- and C-terminal domains, the catalytic tetrad comprises residues Y156, K160, S143, and N115 |
724129 |
| 1.1.1.269 | more |
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 |
-, 762714 |
