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EC Number
Substrates
Commentary Substrates
Organism
Products
Commentary (Products)
Reversibility
1.1.1.269
(2S)-2-hydroxypropyl-CoM + NAD+
-
Xanthobacter autotrophicus
2-oxopropyl-CoM + NADH + H+
-
r
1.1.1.269
(2S)-2-hydroxypropyl-CoM + NAD+
substrate binding structure, overview
Xanthobacter autotrophicus
2-oxopropyl-CoM + NADH + H+
-
r
1.1.1.269
(2S)-2-hydroxypropyl-CoM + NAD+
-
Xanthobacter autotrophicus ATCC BAA-1158
2-oxopropyl-CoM + NADH + H+
-
r
1.1.1.269
(2S)-2-hydroxypropyl-CoM + NAD+
substrate binding structure, overview
Xanthobacter autotrophicus ATCC BAA-1158
2-oxopropyl-CoM + NADH + H+
-
r
1.1.1.269
(R)-2-butanol + NAD+
-
Xanthobacter autotrophicus
2-butanone + NADH + H+
-
r
1.1.1.269
(S)-2-butanol + NAD+
-
Xanthobacter autotrophicus
2-butanone + NADH + H+
-
r
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
1.1.1.269
2-(R)-hydroxypropyl-CoM + NAD+
-
Xanthobacter autotrophicus
2-oxopropyl-CoM + NADH + H+
-
r
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
1.1.1.269
2-(S)-hydroxypropyl-CoM + NAD+
-
Xanthobacter autotrophicus
2-oxopropyl-CoM + NADH + H+
-
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