3.7.1.11: cyclohexane-1,2-dione hydrolase
This is an abbreviated version!
For detailed information about cyclohexane-1,2-dione hydrolase, go to the full flat file.
Reaction
Synonyms
Cdh, ThDP-dependent cyclohexane-1,2-dione hydrolase, thiamine diphosphate dependent cyclohexane-1,2-dione hydrolase
ECTree
3.7.1.11 cyclohexane-1,2-dione hydrolaseAdvanced search results
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results (Engineering
Engineering on EC 3.7.1.11 - cyclohexane-1,2-dione hydrolase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
H28A
site-directed mutagenesis, the mutant enzyme is much less able to catalyze the C-C bond formation as the wild-type enzyme, while the ability for C-C bond cleavage is still intact, the H28A variant shows an 8fold decrease in the formation of (R)-phenylacetylcarbinol (12%), but 1,2-diketone cleavage is nearly unaffected (78% conversion)
H28A/N484A
site-directed mutagenesis, the double mutant catalyzes the addition of pyruvate to cyclohexane-1,2-dione, resulting in the formation of a tertiary alcohol, variant H28A/N484A shows acceptable formation of (R)-phenylacetylcarbinol (73%), but conversion toward the cleavage product is decreased by a factor of five (17% conversion), the mutant is also active with 1,2-diketone in contrast to the wild-type enzyme, mutant substrate specificity amd enantioselectivity, overview
H28A
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site-directed mutagenesis, the mutant enzyme is much less able to catalyze the C-C bond formation as the wild-type enzyme, while the ability for C-C bond cleavage is still intact, the H28A variant shows an 8fold decrease in the formation of (R)-phenylacetylcarbinol (12%), but 1,2-diketone cleavage is nearly unaffected (78% conversion)
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H28A/N484A
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site-directed mutagenesis, the double mutant catalyzes the addition of pyruvate to cyclohexane-1,2-dione, resulting in the formation of a tertiary alcohol, variant H28A/N484A shows acceptable formation of (R)-phenylacetylcarbinol (73%), but conversion toward the cleavage product is decreased by a factor of five (17% conversion), the mutant is also active with 1,2-diketone in contrast to the wild-type enzyme, mutant substrate specificity amd enantioselectivity, overview
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additional information
additional information
substrate specificities and enantioselectivities of wild-type and mutant enzymes, overview
additional information
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substrate specificities and enantioselectivities of wild-type and mutant enzymes, overview
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