Literature summary for 1.1.1.268 extracted from

Krishnakumar, A.M.; Nocek, B.P.; Clark, D.D.; Ensign, S.A.; Peters, J.W.
Structural basis for stereoselectivity in the (R)- and (S)-hydroxypropylthioethanesulfonate dehydrogenases (2006), Biochemistry, 45, 8831-8840.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
the enzyme is cocrystallized in the presence of (S)-hydroxypropyl-coenzyme M, structure refined to 1.8 A resolution	Xanthobacter autotrophicus

Organism

Organism	UniProt	Comment	Textmining
Xanthobacter autotrophicus	Q56840	Py2	-

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+	-	?

Subunits

Subunits	Comment	Organism
tetramer	the tetramer is stabilized by the interaction of the terminal carboxylates of each subunit with divalent metal ions	Xanthobacter autotrophicus

Synonyms

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

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Xanthobacter autotrophicus

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Release 2023.1 (January 2023)