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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

Reaction

bornane-2,6-dione
+
H2O
=
[(1S)-4-hydroxy-2,2,3-trimethylcyclopent-3-enyl]acetate

Synonyms

6-oxo camphor hydrolase, CaMK, OCH, retro-Claisenase

ECTree

     3 Hydrolases
         3.7 Acting on carbon-carbon bonds
             3.7.1 In ketonic substances
                3.7.1.18 6-oxocamphor hydrolase

Engineering

Engineering on EC 3.7.1.18 - 6-oxocamphor hydrolase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
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
-