Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.1.269 extracted from

  • Clark, D.D.
    Characterization of the recombinant (R)- and (S)-hydroxypropyl-coenzyme M dehydrogenases A case study to augment the teaching of enzyme kinetics and stereoselectivity (2019), Biochem. Mol. Biol. Educ., 47, 124-132 .
    View publication on PubMed
Search for more literature for 1.1.1.269

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant enzyme, X-ray diffraction structure determination and analysis Xanthobacter autotrophicus

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Xanthobacter autotrophicus Q56841
-
-
Xanthobacter autotrophicus ATCC BAA-1158 Q56841
-
-

Reaction

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
a

Substrates and Products (Substrate)

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

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

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Xanthobacter autotrophicus
NADH
-
 Xanthobacter autotrophicus

General Information

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