1.1.1.269	(2S)-2-hydroxypropyl-CoM + NAD+	-	Xanthobacter autotrophicus	2-oxopropyl-CoM + NADH + H+	-	r	460039	
1.1.1.269	(2S)-2-hydroxypropyl-CoM + NAD+	substrate binding structure, overview	Xanthobacter autotrophicus	2-oxopropyl-CoM + NADH + H+	-	r	460039	
1.1.1.269	(2S)-2-hydroxypropyl-CoM + NAD+	-	Xanthobacter autotrophicus ATCC BAA-1158	2-oxopropyl-CoM + NADH + H+	-	r	460039	
1.1.1.269	(2S)-2-hydroxypropyl-CoM + NAD+	substrate binding structure, overview	Xanthobacter autotrophicus ATCC BAA-1158	2-oxopropyl-CoM + NADH + H+	-	r	460039	
1.1.1.269	(R)-2-butanol + NAD+	-	Xanthobacter autotrophicus	2-butanone + NADH + H+	-	r	371387	
1.1.1.269	(S)-2-butanol + NAD+	-	Xanthobacter autotrophicus	2-butanone + NADH + H+	-	r	371406	
1.1.1.269	2-(2-hydroxyethylthio)ethanesulfonate + NAD+	achiral mimic of both R-hydroxypropyl-CoM and S-hydroxypropyl-CoM, substrate for both the R- and S-HPCDH enzymes with identical Km values	Xanthobacter autotrophicus	2-(formylmethylthio)ethanesulfonate + NADH + H+	-	r	413908	
1.1.1.269	2-(R)-hydroxypropyl-CoM + NAD+	-	Xanthobacter autotrophicus	2-oxopropyl-CoM + NADH + H+	-	r	383639	
1.1.1.269	2-(R)-hydroxypropyl-CoM + NAD+	poor substrate. S-HPCDH3 cannot bind hydroxypropyl-CoM with CoM oriented properly in the sulfonate-binding pocket that consists of residues R211 and K214. R-hydroxypropyl-CoM binds to S-HPCDH3 with a 290-fold lower affinity but in an orientation where the hydroxyl and hydrogen on C2 can be more properly aligned with tyrosine 156 and NAD+, such that kcat decreases by 4.5-fold relative to the natural substrate S-hydroxypropyl-CoM	Xanthobacter autotrophicus	2-oxopropyl-CoM + NADH + H+	-	r	383639	
1.1.1.269	2-(S)-hydroxypropyl-CoM + NAD+	-	Xanthobacter autotrophicus	2-oxopropyl-CoM + NADH + H+	-	?	383640