6-oxocamphor hydrolase (OCH)

6-oxocamphor hydrolase (OCH) is an enzyme from the crotonase superfamily, found in Rhodococcus species, that catalyzes the carbon–carbon bond cleavage in bicyclic beta-diketones such as 6-oxocamphor, converting them into optically active keto acids via an enzymatic retro-Claisen reaction[1][2][3][6]. Its systematic name is bornane-2,6-dione hydrolase; the enzyme's activity involves converting bornane-2,6-dione and water to yield [(1S)-4-hydroxy-2,2,3-trimethylcyclopent-3-enyl]acetate[2][6]. Structurally, OCH functions as a dimer of trimers and contains active site residues essential for catalysis and prochiral selectivity[1][3]. OCH is not a human drug target and is not known to be involved in human health or disease, but rather is significant in microbial metabolism and potential biocatalytic applications[1][2][5]. Key caveat: No information supports its role as a therapeutic, diagnostic, or disease-relevant target in humans or clinical medicine. If the query relates to human pharmacology or disease, this is not an established target[1][2][5].

Other names

Beta-diketone hydrolaseBornane-2,6-dione hydrolaseEC 3.7.1.18camK (gene)

Enzymatic base-catalyzed cleavage of C–C bonds in substrates such as 6-oxocamphor via a retro-Claisen reaction[1][3][4][5] Involvement of active site residues (notably His-45, His-122, His-145, Asp-154, Glu-244) in catalysis[1][3][4]