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(2R)-2-butanol + NAD+
2-butanone + NADH + H+
Substrates: -
Products: -
r
(2R)-2-heptanol + NAD+
2-heptanone + NADH + H+
Substrates: -
Products: -
r
(2R)-2-hexanol + NAD+
2-hexanone + NADH + H+
Substrates: -
Products: -
r
(2R)-2-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
(2R)-2-octanol + NAD+
2-octanone + NADH + H+
Substrates: -
Products: -
r
(2R)-2-pentanol + NAD+
2-pentanone + NADH + H+
Substrates: -
Products: -
r
(2S)-2-butanol + NAD+
2-butanone + NADH + H+
Substrates: very low activity
Products: -
r
(2S)-2-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
(2S)-2-pentanol + NAD+
2-pentanone + NADH + H+
Substrates: -
Products: -
r
(R)-2-butanol + NAD+
2-butanone + NADH + H+
(R)-2-heptanol + NAD+
2-heptanone + NADH + H+
-
Substrates: -
Products: -
?
(R)-2-hexanol + NAD+
2-hexanone + NADH + H+
-
Substrates: -
Products: -
?
(R)-2-octanol + NAD+
2-octanone + NADH + H+
-
Substrates: -
Products: -
?
(R)-2-pentanol + NAD+
2-pentanone + NADH + H+
-
Substrates: -
Products: -
?
(S)-2-butanol + NAD+
2-butanone + NADH + H+
(S)-2-pentanol + NAD+
2-pentanone + NADH + H+
-
Substrates: -
Products: -
?
2-(2-hydroxyethylthio)ethanesulfonate + NAD+
2-(2-oxoethylthio)ethanesulfonate + NADH
2-(2-hydroxyethylthio)ethanesulfonate + NAD+
2-(formylmethylthio)ethanesulfonate + NADH + H+
Substrates: achiral mimic of both R-hydroxypropyl-CoM and S-hydroxypropyl-CoM, substrate for both the R- and S-HPCDH enzymes with identical Km values
Products: -
r
2-(2-hydroxyethylthio)ethanesulfonate + NADH + H+
?
Substrates: very low activity
Products: -
?
2-(R)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH
2-(R)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
2-(S)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: oxidation of S-hydroxypropyl-CoM with a kcat that is 402 times less than that for R-hydroxypropyl-CoM
Products: -
r
2-butanone + NADH + H+
(2R)-2-butanol + NAD+
Substrates: with no additives present, all forms of recombinant R-HPCDH prefer a re-face hydride addition to produce an enantiomeric excess (EE) of (S)-2-butanol, S- and R-2-butanol are comparably good substrates for the reverse reaction. The sulfonate of ethanesulfonate interacts with R152 and R196 in the CoM binding pocket alongside 2-butanone, in a way that discourages a si-face hydride addition to produce (R)-2-butanol
Products: -
r
2-butanone + NADH + H+
(2S)-2-butanol + NAD+
Substrates: with no additives present, all forms of recombinant R-HPCDH prefer a re-face hydride addition to produce an enantiomeric excess (EE) of (S)-2-butanol, S- and R-2-butanol are comparably good substrates for the reverse reaction. The sulfonate of ethanesulfonate interacts with R152 and R196 in the CoM binding pocket alongside 2-butanone, in a way that discourages a si-face hydride addition to produce (R)-2-butanol
Products: -
r
2-butanone + NADH + H+
(S)-2-butanol + (R)-2-butanol + NAD+
Substrates: -
Products: without additions, 71.9% (S)-enantiomer + 28% (R)-enantiomer, in presence of 1 mM ethansulfonate 92.7% (S)-enantiomer + 7.3% (R)-enantiomer
r
2-oxopropyl-CoM + NADH + H+
2-(R)-hydroxypropyl-CoM + NAD+
Substrates: -
Products: -
r
2-propanol + NAD+
2-propanone + NADH + H+
2-propanol + NAD+
acetone + NADH + H+
-
Substrates: -
Products: -
?
2-[(R)-2-hydroxypropylthio]ethanesulfonate + NAD+
2-(2-ketopropylthio)ethanesulfonate + NADH + H+
-
Substrates: the enzyme is highly specific for the R-enantiomer
Products: -
r
2-[(S)-2-hydroxypropylthio]ethanesulfonate + NAD+
2-(2-ketopropylthio)ethanesulfonate + NADH + H+
-
Substrates: the enzyme is highly specific for the R-enantiomer
Products: -
r
additional information
?
-
(2R)-2-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: -
Products: -
r
(2R)-2-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: substrate binding structure, overview
Products: -
r
(2R)-2-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: -
Products: -
r
(2R)-2-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: substrate binding structure, overview
Products: -
r
(2S)-2-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: competitive inhibitor to the R-enantiomer of substrate, very low activity
Products: -
r
(2S)-2-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: competitive inhibitor to the R-enantiomer of substrate, very low activity
Products: -
r
(R)-2-butanol + NAD+
2-butanone + NADH + H+
Substrates: -
Products: -
r
(R)-2-butanol + NAD+
2-butanone + NADH + H+
-
Substrates: the enantiomeric selectivity of the reverse reaction is 39.6% for (S)-2-butanol without additive, 90.8% with 1 mM CH3CH2SO3-Na+ as additive, 87.8% with 1 mM HSCH2CH2SO3-Na+ as additive, 52.0% with 1 mM CH3CH2COO-Na+ as additive, 46.6% with 1 mM CH3COO-Na+ as additive, 44.8% with 1 mM CH3CH2NH3+Cl- as additive, 45.4% with 1 mM CH3CH2OH as additive, 45.8% with 1 mM Na2SO4 as additive and 40.4% with 1 mM NaCl as additive
Products: -
r
(S)-2-butanol + NAD+
2-butanone + NADH + H+
-
Substrates: -
Products: -
?
(S)-2-butanol + NAD+
2-butanone + NADH + H+
Substrates: -
Products: -
r
2-(2-hydroxyethylthio)ethanesulfonate + NAD+
2-(2-oxoethylthio)ethanesulfonate + NADH
-
Substrates: -
Products: -
?
2-(2-hydroxyethylthio)ethanesulfonate + NAD+
2-(2-oxoethylthio)ethanesulfonate + NADH
-
Substrates: -
Products: -
?
2-(R)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH
-
Substrates: -
Products: -
?
2-(R)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH
-
Substrates: -
Products: -
r
2-(R)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH
-
Substrates: bacterial propylene metabolism
Products: -
?
2-(R)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH
-
Substrates: -
Products: -
?
2-(R)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH
-
Substrates: -
Products: -
r
2-(R)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH
-
Substrates: bacterial propylene metabolism
Products: -
?
2-(R)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
-
Substrates: -
Products: -
?
2-(R)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: -
Products: -
?
2-(R)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: -
Products: -
r
2-propanol + NAD+
2-propanone + NADH + H+
Substrates: -
Products: -
r
2-propanol + NAD+
2-propanone + NADH + H+
Substrates: -
Products: -
r
additional information
?
-
Substrates: R-HPCDH1 can bind either enantiomer of hydroxypropyl-CoM with the CoM moiety oriented properly in the sulfonate-binding pocket consisting of R152 and R196. A high-affinity ternary complex of S-HPC, NAD+ forms, but the misalignment of the hydrogen and hydroxyl groups on C2 relative to NAD+ and the tyrosine general base results in a 403-fold lower turnover rate for the S-enantiomer
Products: -
?
additional information
?
-
Substrates: substrate specificity of the stereochemically different isozymes, R- and S-HPCDH (EC 1.1.1.269) are 41% identical to each other, overview. No activity with (S)-2-hexanol, (S)-2-heptanol, and (S)-2-octanol. Stereochemistry of products from reaction with wild-type and mutant enzymes with or without addition of additives, i.e. CH3CH2SO3- Na+, HSCH2CH2SO3- Na+, CH3CH2COO- Na+, CH3COO- Na+, CH3CH2NH3 +Cl-, CH3CH2OH, Na2SO4, and NaCl, overview
Products: -
-
additional information
?
-
Substrates: substrate specificity of the stereochemically different isozymes, R- and S-HPCDH (EC 1.1.1.269) are 41% identical to each other, overview. No activity with (S)-2-hexanol, (S)-2-heptanol, and (S)-2-octanol. Stereochemistry of products from reaction with wild-type and mutant enzymes with or without addition of additives, i.e. CH3CH2SO3- Na+, HSCH2CH2SO3- Na+, CH3CH2COO- Na+, CH3COO- Na+, CH3CH2NH3 +Cl-, CH3CH2OH, Na2SO4, and NaCl, overview
Products: -
-
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326
(2R)-2-butanol
recombinant enzyme, pH and temperature not specified in the publication
-
2.64
(2R)-2-heptanol
recombinant enzyme, pH and temperature not specified in the publication
-
4.6
(2R)-2-hexanol
recombinant enzyme, pH and temperature not specified in the publication
-
0.102
(2R)-2-hydroxypropyl-CoM
recombinant enzyme, pH and temperature not specified in the publication
-
1.08
(2R)-2-octanol
recombinant enzyme, pH and temperature not specified in the publication
-
20
(2R)-2-pentanol
recombinant enzyme, pH and temperature not specified in the publication
-
315
(2S)-2-butanol
recombinant enzyme, pH and temperature not specified in the publication
-
0.1
(2S)-2-hydroxypropyl-CoM
recombinant enzyme, pH and temperature not specified in the publication
153
(2S)-2-pentanol
recombinant enzyme, pH and temperature not specified in the publication
-
2.64
(R)-2-heptanol
-
pH 7.5, 30°C
4.6
(R)-2-hexanol
-
pH 7.5, 30°C
1.08
(R)-2-octanol
-
pH 7.5, 30°C
20
(R)-2-pentanol
-
pH 7.5, 30°C
153
(S)-2-pentanol
-
pH 7.5, 30°C
0.75 - 0.96
2-(2-hydroxyethylthio)ethanesulfonate
0.092 - 0.44
2-(2-ketopropylthio)ethanesulfonate
0.096 - 0.124
2-(R)-hydroxypropyl-CoM
0.22
2-(S)-hydroxypropyl-CoM
pH 7.5, 30°C
0.068
2-oxopropyl-CoM
pH 7.5, 30°C
0.102
2-[(R)-2-hydroxypropylthio]ethanesulfonate
-
pH 7.5, 30°C
0.1
2-[(S)-2-hydroxypropylthio]ethanesulfonate
-
pH 7.5, 30°C
additional information
additional information
steady-state kinetics, comparison of steady-state kinetics with wild-type an d mutant enzymes, overview
-
220
(R)-2-butanol
pH 7.5, 30°C
328
(R)-2-butanol
-
pH 7.5, 30°C
315
(S)-2-butanol
-
pH 7.5, 30°C
350
(S)-2-butanol
pH 7.5, 30°C
0.75
2-(2-hydroxyethylthio)ethanesulfonate
recombinant enzyme, pH and temperature not specified in the publication
0.96
2-(2-hydroxyethylthio)ethanesulfonate
pH 7.5, 30°C
0.092
2-(2-ketopropylthio)ethanesulfonate
-
pH 7.5, 30°C, wild-type enzyme
0.44
2-(2-ketopropylthio)ethanesulfonate
-
pH 7.5, 30°C, mutant enzyme R209A
0.096
2-(R)-hydroxypropyl-CoM
pH 7.5, 30°C
0.124
2-(R)-hydroxypropyl-CoM
pH 7.4, 30°C
2 - 3
2-butanone
-
pH 7.5, 30°C, mutant enzyme R196A
39
2-butanone
-
pH 7.5, 30°C, mutant enzyme R203A
41
2-butanone
-
pH 7.5, 30°C, mutant enzyme R152A
52
2-butanone
-
pH 7.5, 30°C, wild-type enzyme
84
2-butanone
-
pH 7.5, 30°C, mutant enzyme R209A
1726
2-propanol
-
pH 7.5, 30°C
1726
2-propanol
recombinant enzyme, pH and temperature not specified in the publication
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0.98
(2R)-2-butanol
recombinant enzyme, pH and temperature not specified in the publication
-
1.8
(2R)-2-heptanol
recombinant enzyme, pH and temperature not specified in the publication
-
2.7
(2R)-2-hexanol
recombinant enzyme, pH and temperature not specified in the publication
-
26.8
(2R)-2-hydroxypropyl-CoM
recombinant enzyme, pH and temperature not specified in the publication
-
1.7
(2R)-2-octanol
recombinant enzyme, pH and temperature not specified in the publication
-
1.1
(2R)-2-pentanol
recombinant enzyme, pH and temperature not specified in the publication
-
2.2
(2S)-2-butanol
recombinant enzyme, pH and temperature not specified in the publication
-
0.044
(2S)-2-hydroxypropyl-CoM
recombinant enzyme, pH and temperature not specified in the publication
2.9
(2S)-2-pentanol
recombinant enzyme, pH and temperature not specified in the publication
-
1.8
(R)-2-heptanol
-
pH 7.5, 30°C
2.7
(R)-2-hexanol
-
pH 7.5, 30°C
1.7
(R)-2-octanol
-
pH 7.5, 30°C
1.1
(R)-2-pentanol
-
pH 7.5, 30°C
2.9
(S)-2-pentanol
-
pH 7.5, 30°C
0.29 - 0.55
2-(2-hydroxyethylthio)ethanesulfonate
1.4 - 27.9
2-(2-ketopropylthio)ethanesulfonate
25.8 - 49
2-(R)-hydroxypropyl-CoM
0.12
2-(S)-hydroxypropyl-CoM
pH 7.5, 30°C
24.5 - 29
2-oxopropyl-CoM
26.8
2-[(R)-2-hydroxypropylthio]ethanesulfonate
-
pH 7.5, 30°C
0.044
2-[(S)-2-hydroxypropylthio]ethanesulfonate
-
pH 7.5, 30°C
0.98
(R)-2-butanol
-
pH 7.5, 30°C
1.9
(R)-2-butanol
pH 7.5, 30°C
2.2
(S)-2-butanol
-
pH 7.5, 30°C
9.3
(S)-2-butanol
pH 7.5, 30°C
0.29
2-(2-hydroxyethylthio)ethanesulfonate
-
-
0.29
2-(2-hydroxyethylthio)ethanesulfonate
recombinant enzyme, pH and temperature not specified in the publication
0.55
2-(2-hydroxyethylthio)ethanesulfonate
pH 7.5, 30°C
1.4
2-(2-ketopropylthio)ethanesulfonate
-
pH 7.5, 30°C, mutant enzyme R152A
2.4
2-(2-ketopropylthio)ethanesulfonate
-
pH 7.5, 30°C, mutant enzyme R196A
15
2-(2-ketopropylthio)ethanesulfonate
-
pH 7.5, 30°C, mutant enzyme R209A
24.5
2-(2-ketopropylthio)ethanesulfonate
-
pH 7.5, 30°C, wild-type enzyme
27.9
2-(2-ketopropylthio)ethanesulfonate
-
pH 7.5, 30°C, mutant enzyme R203A
25.8
2-(R)-hydroxypropyl-CoM
-
-
29
2-(R)-hydroxypropyl-CoM
pH 7.4, 30°C
49
2-(R)-hydroxypropyl-CoM
pH 7.5, 30°C
0.012
2-butanone
-
pH 7.5, 30°C, mutant enzyme R203A
0.027
2-butanone
-
pH 7.5, 30°C, wild-type enzyme
0.028
2-butanone
-
pH 7.5, 30°C, mutant enzyme R152A
0.032
2-butanone
-
pH 7.5, 30°C, mutant enzyme R209A
0.033
2-butanone
-
pH 7.5, 30°C, mutant enzyme R196A
24.5
2-oxopropyl-CoM
-
-
29
2-oxopropyl-CoM
pH 7.5, 30°C
2.9
2-propanol
-
pH 7.5, 30°C
2.9
2-propanol
recombinant enzyme, pH and temperature not specified in the publication
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evolution
the enzyme belongs to the short-chain dehydrogenases/reductase (SDR) superfamily of enzymes. The C-terminal domains of SDR enzymes are responsible for imparting substrate specificity
evolution
-
the enzyme belongs to the short-chain dehydrogenases/reductase (SDR) superfamily of enzymes. The C-terminal domains of SDR enzymes are responsible for imparting substrate specificity
-
malfunction
substitution of R152 or R196 for alanine inhibits ethanesulfonate binding to the extent that its addition does not increase the EE of (S)-2-butanol produced by these mutants
malfunction
-
substitution of R152 or R196 for alanine inhibits ethanesulfonate binding to the extent that its addition does not increase the EE of (S)-2-butanol produced by these mutants
-
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 a common achiral product 2-ketopropyl-CoM
metabolism
(R)- and (S)-hydroxypropyl-coenzyme M dehydrogenase (R- and S-HPCDH), are part of a bacterial pathway of short-chain alkene and epoxide metabolism. R- and S-HPCDH act on different substrate enantiomers in a common pathway
metabolism
-
(R)- and (S)-hydroxypropyl-coenzyme M dehydrogenase (R- and S-HPCDH), are part of a bacterial pathway of short-chain alkene and epoxide metabolism. R- and S-HPCDH act on different substrate enantiomers in a common pathway
-
additional information
-
structural basis for stereospecificity of R-HPCDH, comparison to S-HPCDH, EC 1.1.1.269, 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
additional information
structure-function relationship, active site structure modeling and stereochemistry of reaction mechanism, overview. The C-terminal domains of SDR enzymes are responsible for imparting substrate specificity. Two arginine residues, R152 and R196, play a key role in substrate binding and stereoselectivity of enzyme R-HPCDH. R152 and R196 bind the sulfonate of 2-oxopropyl-CoM (2-KPC)
additional information
-
structure-function relationship, active site structure modeling and stereochemistry of reaction mechanism, overview. The C-terminal domains of SDR enzymes are responsible for imparting substrate specificity. Two arginine residues, R152 and R196, play a key role in substrate binding and stereoselectivity of enzyme R-HPCDH. R152 and R196 bind the sulfonate of 2-oxopropyl-CoM (2-KPC)
-
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R179A
-
no detectable activity with 2-(2-ketopropylthio)ethanesulfonate and 2-butanone
R152A
-
site-directed mutagenesis, the mutant shows altered substrate specificity and interaction with additives compared to wild-type enzyme
-
R196A
-
site-directed mutagenesis, the mutant shows altered substrate specificity and interaction with additives compared to wild-type enzyme
-
R203A
-
site-directed mutagenesis, the mutant shows altered substrate specificity and interaction with additives compared to wild-type enzyme
-
R209A
-
site-directed mutagenesis, the mutant shows altered substrate specificity and interaction with additives compared to wild-type enzyme
-
S142A
-
greatly reduced activity
K159A
-
inactive enzyme
-
S142A
-
greatly reduced activity
-
S142C
-
inactive enzyme
-
Y155E
-
inactive enzyme
-
Y155F
-
inactive enzyme
-
R152A
-
the ratio of turnover number to Km-value for 2-(2-ketopropylthio)ethanesulfonate is 5192fold lower than the ratio for the wild-type enzyme. The ratio of turnover number to Km-value for 2-butanone is 1.3fold higher than the ratio for the wild-type enzyme
R152A
site-directed mutagenesis, the mutant shows altered substrate specificity and interaction with additives compared to wild-type enzyme
R196A
-
the ratio of turnover number to Km-value for 2-(2-ketopropylthio)ethanesulfonate is 1000fold lower than the ratio for the wild-type enzyme. The ratio of turnover number to Km-value for 2-butanone is 2.7fold higher than the ratio for the wild-type enzyme
R196A
site-directed mutagenesis, the mutant shows altered substrate specificity and interaction with additives compared to wild-type enzyme
R203A
-
the ratio of turnover number to Km-value for 2-(2-ketopropylthio)ethanesulfonate is 4.3fold lower than the ratio for the wild-type enzyme. The ratio of turnover number to Km-value for 2-butanone is 1.6fold lower than the ratio for the wild-type enzyme
R203A
site-directed mutagenesis, the mutant shows altered substrate specificity and interaction with additives compared to wild-type enzyme
R209A
-
the ratio of turnover number to Km-value for 2-(2-ketopropylthio)ethanesulfonate is 2.7fold lower than the ratio for the wild-type enzyme. The ratio of turnover number to Km-value for 2-butanone is 1.4fold lower than the ratio for the wild-type enzyme
R209A
site-directed mutagenesis, the mutant shows altered substrate specificity and interaction with additives compared to wild-type enzyme
additional information
comparison of steady-state kinetics and 2-butanol production arte and stereochemistry of wild-type and mutant enzymes, overview
additional information
-
comparison of steady-state kinetics and 2-butanol production arte and stereochemistry of wild-type and mutant enzymes, overview
-
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Allen, J.R.; Clark, D.D.; Krum, J.G.; Ensign, S.A.
A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial pathway of aliphatic epoxide carboxylation
Proc. Natl. Acad. Sci. USA
96
8432-8437
1999
Xanthobacter sp., Xanthobacter sp. Py2
brenda
Clark, D.D.; Ensign, S.A.
Characterization of the 2-[(R)-2-hydroxypropylthio]ethanesulfonate dehydrogenase from Xanthobacter Strain Py2: Product inhibition, pH dependence of kinetic parameters, site-directed mutagenesis, rapid equilibrium inhibition, and chemical modification
Biochemistry
41
2727-2740
2002
Xanthobacter sp., Xanthobacter sp. Py2
brenda
Krum, J.G.; Ensign, S.A.
Evidence that a linear megaplasmid encodes enzymes of aliphatic alkene and epoxide metabolism and coenzyme M (2-mercaptoethanesulfonate) biosynthesis in Xanthobacter strain Py2
J. Bacteriol.
183
2172-2177
2001
Xanthobacter sp., Xanthobacter sp. Py2
brenda
Clark, D.D.; Boyd, J.M.; Ensign, S.A.
The stereoselectivity and catalytic properties of Xanthobacter autotrophicus 2-[(R)-2-hydroxypropylthio]ethanesulfonate dehydrogenase are controlled by interactions between C-terminal arginine residues and the sulfonate of coenzyme M
Biochemistry
43
6763-6771
2004
Xanthobacter autotrophicus
brenda
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
Biochemistry
45
8831-8840
2006
Xanthobacter autotrophicus (Q56840)
brenda
Sliwa, D.A.; Krishnakumar, A.M.; Peters, J.W.; Ensign, S.A.
Molecular basis for enantioselectivity in the (R)- and (S)-hydroxypropylthioethanesulfonate dehydrogenases, a unique pair of stereoselective short-chain dehydrogenases/reductases involved in aliphatic epoxide carboxylation
Biochemistry
49
3487-3498
2010
Xanthobacter autotrophicus (Q56840)
brenda
Boyd, J.M.; Clark, D.D.; Kofoed, M.A.; Ensign, S.A.
Mechanism of inhibition of aliphatic epoxide carboxylation by the coenzyme M analog 2-bromoethanesulfonate
J. Biol. Chem.
285
25232-25242
2010
Xanthobacter autotrophicus (Q56840)
brenda
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
Arch. Biochem. Biophys.
533
62-68
2013
Xanthobacter autotrophicus
brenda
Clark, D.D.
Characterization of the recombinant (R)- and (S)-hydroxypropyl-coenzyme M dehydrogenases A case study to augment the teaching of enzyme kinetics and stereoselectivity
Biochem. Mol. Biol. Educ.
47
124-132
2019
Xanthobacter autotrophicus (Q56840), Xanthobacter autotrophicus ATCC BAA-1158 (Q56840)
brenda