Literature summary for 3.7.1.18 extracted from

Whittingham, J.; Turkenburg, J.; Verma, C.; Walsh, M.; Grogan, G.
The 2-A crystal structure of 6-oxo camphor hydrolase: new structural diversity in the crotonase superfamily (2003), J. Biol. Chem., 278, 1744-1750.

Cloned(Commentary)

Cloned (Comment)	Organism
gene camK, expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) and B8434(DE3) and native and selenomethionine-labeled proteins, respectively	Rhodococcus erythropolis

Crystallization (Commentary)

Crystallization (Comment)	Organism
selenomethionine-labeled enzyme, vapor diffusion hanging drop technique, protein solution containing 10 mg/ml protein in 50 mM Tris-HCl, pH 7.0, 1 mM dithiothreitol, 0.020 mM phenylmethylsulfonyl fluoride is mixed in a 1:1 ratio with reservoir solution, that contains for the native enzyme, the reservoir solution consisted of 0.1 M sodium acetate buffer, pH 4.5, 0.2 M ammonium sulfate, and 28% v/v PEG 4000, and for the selenomethionyl enzyme 0.1 M MES, pH 5.5, 0.2 M ammonium sulfate, 37.5% v/v 5,000 Da monomethyl ether, and 0.2% w/v n-octyl-beta-D-glucopyranoside, X-ray diffraction structure determination and analysis at 2.0-2.4 A resolution, selenomethionine multiple wave anomalous dispersion, molecular modeling	Rhodococcus erythropolis

Crystallization (Comment)

Organism

selenomethionine-labeled enzyme, vapor diffusion hanging drop technique, protein solution containing 10 mg/ml protein in 50 mM Tris-HCl, pH 7.0, 1 mM dithiothreitol, 0.020 mM phenylmethylsulfonyl fluoride is mixed in a 1:1 ratio with reservoir solution, that contains for the native enzyme, the reservoir solution consisted of 0.1 M sodium acetate buffer, pH 4.5, 0.2 M ammonium sulfate, and 28% v/v PEG 4000, and for the selenomethionyl enzyme 0.1 M MES, pH 5.5, 0.2 M ammonium sulfate, 37.5% v/v 5,000 Da monomethyl ether, and 0.2% w/v n-octyl-beta-D-glucopyranoside, X-ray diffraction structure determination and analysis at 2.0-2.4 A resolution, selenomethionine multiple wave anomalous dispersion, molecular modeling

Rhodococcus erythropolis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Rhodococcus erythropolis	6-oxo camphor hydrolase catalyzes carbon-carbon bond cleavage in bicyclic beta-diketones via a retro-Claisen reaction	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Rhodococcus erythropolis	-	gene camK	-

Reaction

Reaction	Comment	Organism	Reaction ID
bornane-2,6-dione + H2O = [(1S)-4-hydroxy-2,2,3-trimethylcyclopent-3-enyl]acetate	mechanism of carbon-carbon bond cleavage by 6-oxo camphor hydrolase	Rhodococcus erythropolis	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	6-oxo camphor hydrolase catalyzes carbon-carbon bond cleavage in bicyclic beta-diketones via a retro-Claisen reaction	Rhodococcus erythropolis	?	-	?
additional information	modeling of the substrate, 6-oxo camphor, and a proposed enolate intermediate in the putative active site suggesting possible mechanistic roles for Glu244, Asp154, His122, His45, and His145, overview	Rhodococcus erythropolis	?	-	?

Subunits

Subunits	Comment	Organism
hexamer	dimer of trimers, crystal structure, overview	Rhodococcus erythropolis
More	quaternary structure of OCH, overview	Rhodococcus erythropolis

Synonyms

Synonyms	Comment	Organism
6-oxo camphor hydrolase	-	Rhodococcus erythropolis
OCH	-	Rhodococcus erythropolis

General Information

General Information	Comment	Organism
evolution	the 6-oxo camphor hydrolase belongs to the crotonase superfamily, reactions catalyzed by representative members of the crotonase superfamily, overview	Rhodococcus erythropolis
metabolism	the 6-oxocamphor hydrolase is involved in the degeneration of (1 R)-(+)-camphor	Rhodococcus erythropolis