5-Exo-hydroxycamphor dehydrogenase
5-exo-hydroxycamphor dehydrogenase (EC 1.1.1.327, F-dehydrogenase, FdeH) is an enzyme with systematic name 5-exo-hydroxycamphor:NAD+ oxidoreductase.[1][2][3] This enzyme catalyses the following chemical reaction
- 5-exo-hydroxycamphor + NAD+ bornane-2,5-dione + NADH + H+
5-exo-hydroxycamphor dehydrogenase | |||||||||
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Identifiers | |||||||||
EC number | 1.1.1.327 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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This enzyme contains Zn2+. It is isolated from Pseudomonas putida.
References
- Rheinwald JG, Chakrabarty AM, Gunsalus IC (March 1973). "A transmissible plasmid controlling camphor oxidation in Pseudomonas putida". Proceedings of the National Academy of Sciences of the United States of America. 70 (3): 885–9. doi:10.1073/pnas.70.3.885. PMC 433381. PMID 4351810.
- Koga H, Yamaguchi E, Matsunaga K, Aramaki H, Horiuchi T (November 1989). "Cloning and nucleotide sequences of NADH-putidaredoxin reductase gene (camA) and putidaredoxin gene (camB) involved in cytochrome P-450cam hydroxylase of Pseudomonas putida". Journal of Biochemistry. 106 (5): 831–6. doi:10.1093/oxfordjournals.jbchem.a122939. PMID 2613690.
- Aramaki H, Koga H, Sagara Y, Hosoi M, Horiuchi T (July 1993). "Complete nucleotide sequence of the 5-exo-hydroxycamphor dehydrogenase gene on the CAM plasmid of Pseudomonas putida (ATCC 17453)". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1174 (1): 91–4. doi:10.1016/0167-4781(93)90098-x. PMID 8334169.
External links
- 5-exo-hydroxycamphor+dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH)
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