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
ECTree
1.1.1.268 2-(R)-hydroxypropyl-CoM dehydrogenaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.1.1.268 - 2-(R)-hydroxypropyl-CoM dehydrogenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
R152A
R179A
-
no detectable activity with 2-(2-ketopropylthio)ethanesulfonate and 2-butanone
R196A
R203A
R209A
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
-
additional information
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
-
