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Literature summary for 1.1.1.268 extracted from

  • Bakelar, J.W.; Sliwa, D.A.; Johnson, S.J.
    Crystal structures of S-HPCDH reveal determinants of stereospecificity for R- and S-hydroxypropyl-coenzyme M dehydrogenases (2013), Arch. Biochem. Biophys., 533, 62-68.
    View publication on PubMed
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Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Xanthobacter autotrophicus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-(R)-hydroxypropyl-CoM + NAD+
-
 Xanthobacter autotrophicus 2-oxopropyl-CoM + NADH + H+
-
 ?

Synonyms

Synonyms Comment Organism
(R)-hydroxypropyl-coenzyme M dehydrogenase
-
 Xanthobacter autotrophicus
R-HPCDH
-
 Xanthobacter autotrophicus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Xanthobacter autotrophicus

General Information

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