1.1.1.269: 2-(S)-hydroxypropyl-CoM dehydrogenase
This is an abbreviated version!
For detailed information about 2-(S)-hydroxypropyl-CoM dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.269
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1.1.1.269
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epoxide
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stereoselectivity
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autotrophicus
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xanthobacter
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achiral
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s-enantiomers
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ketones
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enantioselectivity
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product-bound
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propylene
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epoxypropane
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acetoacetate
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2-butanone
- 1.1.1.269
- epoxide
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stereoselectivity
- autotrophicus
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xanthobacter
-
achiral
-
s-enantiomers
- ketones
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enantioselectivity
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product-bound
- propylene
- epoxypropane
- acetoacetate
- 2-butanone
Reaction
Synonyms
(S)-hydroxypropyl-coenzyme M dehydrogenase, (S)-hydroxypropylthioethanesulfonate dehydrogenase, 2-(2-(S)-hydroxypropylthio)ethanesulfonate dehydrogenase, HPCDH3, S-HPCDH, xecE, xecE1, xecE3
ECTree
1.1.1.269 2-(S)-hydroxypropyl-CoM dehydrogenaseAdvanced search results
results (
results (Results
in table
189
17
15
Substrates Products
Substrates Products on EC 1.1.1.269 - 2-(S)-hydroxypropyl-CoM dehydrogenase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-(2-hydroxyethylthio)ethanesulfonate + NAD+
2-(formylmethylthio)ethanesulfonate + NADH + H+
achiral mimic of both R-hydroxypropyl-CoM and S-hydroxypropyl-CoM, substrate for both the R- and S-HPCDH enzymes with identical Km values
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-
r
2-oxopropyl-CoM + NADH + H+
2-(R)-hydroxypropyl-CoM + NAD+
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-
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r
(2S)-2-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
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-
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r
(2S)-2-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
substrate binding structure, overview
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-
r
(2S)-2-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
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-
-
r
(2S)-2-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
substrate binding structure, overview
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-
r
2-(R)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
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-
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r
2-(R)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
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
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-
r
2-(S)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
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-
-
-
?
2-(S)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
-
-
-
r
2-(S)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
-
-
-
?
2-(S)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
substrate binding structures, overview
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-
?
2-(S)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
oxidation of S-hydroxypropyl-CoM with a kcat that is 402 times less than that for R-hydroxypropyl-CoM
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r
2-(S)hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH
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involved in propylene metabolism in bacteria
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?
2-(S)hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH
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involved in propylene metabolism in bacteria
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?
2-butanone + NADH + H+
(S)-2-butanol + (R)-2-butanol + NAD+
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-
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r
2-butanone + NADH + H+
(S)-2-butanol + (R)-2-butanol + NAD+
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without additions, 99.2% (S)-enantiomer + 0.8% (R)-enantiomer, in presence of 1 mM ethansulfonate 99.0% (S)-enantiomer + 2% (R)-enantiomer. Mutant K214A, without additions, 91.6% (S)-enantiomer + 8.4% (R)-enantiomer, in presence of 1 mM ethansulfonate 90.9% (S)-enantiomer + 9.1% (R)-enantiomer
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r
additional information
?
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substrate specificity of the stereochemically different isozymes, R-HPCDH (EC 1.1.1.268) and S-HPCDH are 41% identical to each other, overview
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-
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additional information
?
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substrate specificity of the stereochemically different isozymes, R-HPCDH (EC 1.1.1.268) and S-HPCDH are 41% identical to each other, overview
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