Literature summary for 1.1.1.269 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.

Search for more literature for 1.1.1.269

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant S-HPCDH free or bound to substrates 2-(S)-hydroxypropyl-CoM and NAD+, sitting drop vapour diffusion method, mixing of equal volumes of 13 mg/ml protein in buffer containing 25% glycerol, with or without 0.05 mM NAD+ and 0.05 mM 2-(S)-hydroxypropyl-CoM, with well solution containing of 0.1 M Bis-Tris, pH 6.5, 0.35 M ammonium acetate and 27% PEG 3350, X-ray diffraction structure determination and analysis at 1.60 A resolution	Xanthobacter autotrophicus

Crystallization (Comment)

Organism

purified recombinant S-HPCDH free or bound to substrates 2-(S)-hydroxypropyl-CoM and NAD+, sitting drop vapour diffusion method, mixing of equal volumes of 13 mg/ml protein in buffer containing 25% glycerol, with or without 0.05 mM NAD+ and 0.05 mM 2-(S)-hydroxypropyl-CoM, with well solution containing of 0.1 M Bis-Tris, pH 6.5, 0.35 M ammonium acetate and 27% PEG 3350, X-ray diffraction structure determination and analysis at 1.60 A resolution

Xanthobacter autotrophicus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
2-(S)-hydroxypropyl-CoM + NAD+	Xanthobacter autotrophicus	-	2-oxopropyl-CoM + NADH + H+	-	?

Organism

Organism	UniProt	Comment	Textmining
Xanthobacter autotrophicus	A7IQH5	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2-(S)-hydroxypropyl-CoM + NAD+	-	Xanthobacter autotrophicus	2-oxopropyl-CoM + NADH + H+	-	?
2-(S)-hydroxypropyl-CoM + NAD+	substrate binding structures, overview	Xanthobacter autotrophicus	2-oxopropyl-CoM + NADH + H+	-	?

Synonyms

Synonyms	Comment	Organism
(S)-hydroxypropyl-coenzyme M dehydrogenase	-	Xanthobacter autotrophicus
S-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 acommon achiral product 2-ketopropyl-CoM	Xanthobacter autotrophicus
additional information	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	Xanthobacter autotrophicus