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Enzyme Nomenclature
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
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EC NUMBER 
COMMENTARY 
1.1.1.269
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RECOMMENDED NAME
GeneOntology No.
2-(S)-hydroxypropyl-CoM dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-(S)-hydroxypropyl-CoM + NAD+ = 2-oxopropyl-CoM + NADH + H+
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
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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CAS REGISTRY NUMBER
COMMENTARY
369364-40-9
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
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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-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
2-oxopropyl-CoM + NADH + H+
2-(R)-hydroxypropyl-CoM + NAD+
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r
2-(R)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
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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+
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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+
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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?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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-(S)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
A7IQH5
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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-(S)hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH
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involved in propylene metabolism in bacteria
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanesulfonate
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i.e. coenzyme M: function in catabolic pathway of hydrocarbon oxidation
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-(2-methyl-2-hydroxypropylthio)ethanesulfonate
competitive; competitive
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.97
2-(2-hydroxyethylthio)ethanesulfonate
wild-type, pH 7.5, 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.8
2-(2-hydroxyethylthio)ethanesulfonate
wild-type, pH 7.5, 30°C
1.7
2-propanol
mutant K214A, pH 7.5, 30°C; mutant R211A, pH 7.5, 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.29
2-(2-methyl-2-hydroxypropylthio)ethanesulfonate
pH 7.5, 30°C; wild-type, pH 7.5, 30°C
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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metabolism of propylene depends on the presence of a linear megaplasmid, that encodes enzymes of alkene oxidation, epoxide carboxylation and CoM biosynthesis
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metabolism of propylene depends on the presence of a linear megaplasmid, that encodes enzymes of alkene oxidation, epoxide carboxylation and CoM biosynthesis
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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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli; expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
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
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.269)
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