3.7.1.18: 6-oxocamphor hydrolase
This is an abbreviated version!
For detailed information about 6-oxocamphor hydrolase, go to the full flat file.
Word Map on EC 3.7.1.18
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3.7.1.18
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crotonase
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desymmetrization
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beta-diketones
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bicyclic
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diketone
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rhodococcus
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ncimb
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prochiral
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enol
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hexamer
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anabaena
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trimer
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dyad
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carbon-carbon
- 3.7.1.18
- crotonase
-
desymmetrization
- beta-diketones
-
bicyclic
- diketone
- rhodococcus
-
ncimb
-
prochiral
-
enol
-
hexamer
- anabaena
- trimer
-
dyad
-
carbon-carbon
Reaction
Synonyms
6-oxo camphor hydrolase, CaMK, OCH, retro-Claisenase
ECTree
Advanced search results
Engineering
Engineering on EC 3.7.1.18 - 6-oxocamphor hydrolase
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D154N
site-directed mutagenesis, the OCH mutant shows a greatly reduced value of kcat/Km derived from a very large increase in Km for the native substrate 6-oxo camphor compared to the wild-type enzyme
E244Q
site-directed mutagenesis, the mutant shows reduced value of kcat/Km compared to the wild-type enzyme
H122A
site-directed mutagenesis, structure analysis and comparison to the wild-type enzyme, the mutant shows a greatly reduced value of kcat, and its Km is five times that of the wild-type enzyme. The H122A mutant forms a hexamer, a dimer of trimers, identical to that of the wild-type enzyme
H145A
site-directed mutagenesis, the OCH mutant shows a greatly reduced value of kcat/Km derived from a very large increase in Km for the native substrate 6-oxo camphor compared to the wild-type enzyme
H45A
site-directed mutagenesis, the mutant shows reduced value of kcat/Km compared to the wild-type enzyme
D154N
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site-directed mutagenesis, the OCH mutant shows a greatly reduced value of kcat/Km derived from a very large increase in Km for the native substrate 6-oxo camphor compared to the wild-type enzyme
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E244Q
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site-directed mutagenesis, the mutant shows reduced value of kcat/Km compared to the wild-type enzyme
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H122A
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site-directed mutagenesis, structure analysis and comparison to the wild-type enzyme, the mutant shows a greatly reduced value of kcat, and its Km is five times that of the wild-type enzyme. The H122A mutant forms a hexamer, a dimer of trimers, identical to that of the wild-type enzyme
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H145A
-
site-directed mutagenesis, the OCH mutant shows a greatly reduced value of kcat/Km derived from a very large increase in Km for the native substrate 6-oxo camphor compared to the wild-type enzyme
-
H45A
-
site-directed mutagenesis, the mutant shows reduced value of kcat/Km compared to the wild-type enzyme
-