5-exo-hydroxycamphor dehydrogenase (camD)

5-exo-hydroxycamphor dehydrogenase is a bacterial enzyme, primarily characterized in Pseudomonas putida, that plays a vital role in the degradation of camphor [1]. It is encoded by the camD gene and belongs to the short-chain dehydrogenase/reductase (SDR) superfamily [1, 3]. The enzyme specifically catalyzes the NAD+-dependent oxidation of 5-exo-hydroxycamphor to form 2,5-diketocamphane, which is a necessary step for the bacterium to utilize camphor as a sole carbon and energy source [2, 3]. While it is a well-studied model for understanding enzyme specificity and microbial metabolic operons, it is not currently recognized as a therapeutic target for human diseases [1, 2]. The enzyme exhibits high stereospecificity, favoring the exo-isomer of its substrate over the endo-isomer [2]. Its primary significance lies in the fields of environmental microbiology, bioremediation, and potential applications in industrial biocatalysis [2, 3]. Structural analysis has confirmed its reliance on the NAD+ cofactor for its catalytic mechanism [1].

Other names

5-hydroxycamphor dehydrogenaseexo-5-hydroxycamphor dehydrogenasecamD5-exo-hydroxycamphor:NAD+ oxidoreductase

Catalyzes the NAD+-dependent oxidation of 5-exo-hydroxycamphor to 2,5-diketocamphane as part of the camphor catabolic pathway.