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
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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
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General Information
General Information on EC 1.1.1.269 - 2-(S)-hydroxypropyl-CoM dehydrogenase
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evolution
metabolism
additional information
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
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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
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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
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
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(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
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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
additional information
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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
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
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
-