EC Number   |
General Information |
Reference |
|---|
  1.1.1.268 | 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 |
| 1.1.1.268 | malfunction |
substitution of R152 or R196 for alanine inhibits ethanesulfonate binding to the extent that its addition does not increase the EE of (S)-2-butanol produced by these mutants |
-, 762714 |
| 1.1.1.268 | 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 |
| 1.1.1.268 | 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 |
724129 |
| 1.1.1.268 | more |
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 |
724129 |
| 1.1.1.268 | 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. Two arginine residues, R152 and R196, play a key role in substrate binding and stereoselectivity of enzyme R-HPCDH. R152 and R196 bind the sulfonate of 2-oxopropyl-CoM (2-KPC) |
-, 762714 |
