Information on EC 1.1.1.269 - 2-(S)-hydroxypropyl-CoM dehydrogenase

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The expected taxonomic range for this enzyme is: Xanthobacter

EC NUMBER
COMMENTARY hide
1.1.1.269
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RECOMMENDED NAME
GeneOntology No.
2-(S)-hydroxypropyl-CoM dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-(S)-hydroxypropyl-CoM + NAD+ = 2-oxopropyl-CoM + NADH + H+
show the reaction diagram
highly specific; The enzyme is highly specific for (S)-2-hydroxyalkyl thioethers of CoM, in contrast to EC 1.1.1.268, 2-(R)-hydroxypropyl-CoM dehydrogenase, which is highly specific of the (R)-enantiomer. This enzyme forms component IV of four-component enzyme system. Comprising EC 4.2.99.19, 2-hydroxypropyl-CoM lyase, component I, EC 1.8.1.5, 2-oxopropyl-CoM reductase, carboxylating, component II, EC 1.1.1.268, 2-(R)-hydroxypropyl-CoM dehydrogenase, component III, and EC 1.1.1.269, 2-(S)-hydroxypropyl-CoM dehydrogenase, component IV, that is involved in epoxylalkane carboxylation in Xanthobacter sp. strain Py2
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
propene degradation
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SYSTEMATIC NAME
IUBMB Comments
2-[2-(S)-hydroxypropylthio]ethanesulfonate:NAD+ oxidoreductase
The enzyme is highly specific for (S)-2-hydroxyalkyl thioethers of CoM, in contrast to EC 1.1.1.268, 2-(R)-hydroxypropyl-CoM dehydrogenase, which is highly specific for the (R)-enantiomer. This enzyme forms component IV of a four-component enzyme system {comprising EC 4.4.1.23 (2-hydroxypropyl-CoM lyase; component I), EC 1.8.1.5 [2-oxopropyl-CoM reductase (carboxylating); component II], EC 1.1.1.268 [2-(R)-hydroxypropyl-CoM dehydrogenase; component III] and EC 1.1.1.269 [2-(S)-hydroxypropyl-CoM dehydrogenase; component IV]} that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2.
CAS REGISTRY NUMBER
COMMENTARY hide
369364-40-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain Py2
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Manually annotated by BRENDA team
strain Py2
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-2-butanol + NAD+
2-butanone + NADH + H+
show the reaction diagram
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r
(S)-2-butanol + NAD+
2-butanone + NADH + H+
show the reaction diagram
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r
2-(2-hydroxyethylthio)ethanesulfonate + NAD+
2-(formylmethylthio)ethanesulfonate + NADH + H+
show the reaction diagram
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-(R)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
show the reaction diagram
2-(S)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
show the reaction diagram
2-(S)hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH
show the reaction diagram
2-butanone + NADH + H+
(S)-2-butanol + (R)-2-butanol + NAD+
show the reaction diagram
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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
2-oxopropyl-CoM + NADH + H+
2-(R)-hydroxypropyl-CoM + NAD+
show the reaction diagram
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r
2-propanol + NAD+
acetone + NADH + H+
show the reaction diagram
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r
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-(S)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
show the reaction diagram
A7IQH5
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?
2-(S)hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanesulfonate
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i.e. coenzyme M: function in catabolic pathway of hydrocarbon oxidation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-(2-methyl-2-hydroxypropylthio)ethanesulfonate
competitive; competitive
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
68
(R)-2-butanol
wild-type, pH 7.5, 30C
28
(S)-2-butanol
wild-type, pH 7.5, 30C
0.97
2-(2-hydroxyethylthio)ethanesulfonate
wild-type, pH 7.5, 30C
0.096 - 9.1
2-(R)-hydroxypropyl-CoM
0.031 - 9.5
2-(S)-hydroxypropyl-CoM
72 - 180
2-butanone
0.068 - 12
2-oxopropyl-CoM
720 - 1400
2-propanol
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
(R)-2-butanol
Xanthobacter autotrophicus
Q56841
wild-type, pH 7.5, 30C
2.6
(S)-2-butanol
Xanthobacter autotrophicus
Q56841
wild-type, pH 7.5, 30C
3.8
2-(2-hydroxyethylthio)ethanesulfonate
Xanthobacter autotrophicus
Q56841
wild-type, pH 7.5, 30C
5.5 - 49
2-(R)-hydroxypropyl-CoM
0.013 - 25
2-(S)-hydroxypropyl-CoM
0.039 - 0.072
2-butanone
8.6 - 29
2-oxopropyl-CoM
1.7 - 2
2-propanol
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0148
(R)-2-butanol
Xanthobacter autotrophicus
Q56841
wild-type, pH 7.5, 30C
2292
0.0928
(S)-2-butanol
Xanthobacter autotrophicus
Q56841
wild-type, pH 7.5, 30C
1990
0.6 - 500
2-(R)-hydroxypropyl-CoM
5698
0.0014 - 790
2-(S)-hydroxypropyl-CoM
4101
0.37 - 0.54
2-butanone
1171
0.75 - 420
2-oxopropyl-CoM
3884
1.4 - 2.4
2-propanol
682
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.29
2-(2-methyl-2-hydroxypropylthio)ethanesulfonate
pH 7.5, 30C; wild-type, pH 7.5, 30C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme; recombinant enzyme
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli; expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K214A
substantially reduced catalytic efficiencies with the natural substrates in both the oxidative and reductive direction
R211A
substantially reduced catalytic efficiencies with the natural substrates in both the oxidative and reductive direction
S143A
residue acts as H-bond donor to substrate and in charge stabilization of the transition state, large increase in Km value
Y156A
mutation in general acid/base, large increase in Km value