1.1.1.268: 2-(R)-hydroxypropyl-CoM dehydrogenase
This is an abbreviated version!
For detailed information about 2-(R)-hydroxypropyl-CoM dehydrogenase, go to the full flat file.
Reaction
Synonyms
(R)-hydroxypropyl-coenzyme M dehydrogenase, (R)-hydroxypropylthioethanesulfonate dehydrogenase, 2-(2-(R)-hydroxypropylthio)ethanesulfonate dehydrogenase, 2-(R)-hydroxypropyl-coenzyme M dehydrogenase, R-HPCDH, xecD
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General Information
General Information on EC 1.1.1.268 - 2-(R)-hydroxypropyl-CoM dehydrogenase
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evolution
malfunction
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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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
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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
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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 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
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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 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
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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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