Cytochrome P450 camphor 5-monooxygenase is a bacterial enzyme originally from Pseudomonas putida, which catalyzes a critical step in the metabolism of camphor. In 1987, Cytochrome P450cam was the first cytochrome P450 three-dimensional protein structure solved by X-ray crystallography.[1]
It is a heterotrimeric protein derived from the products of three genes: a cytochrome P450 enzyme (encoded by the CamC gene from the CYP family CYP101), a Putidaredoxin (encoded by the CamB gene) complexed with cofactors 2Fe-2S, a NADH-dependent Putidaredoxin reductase (encoded by the CamA gene).[2]
References
- ↑ Poulos, Thomas L.; Finzel, Barry C.; Howard, Andrew J. (June 1987). "High-resolution crystal structure of cytochrome P450cam". Journal of Molecular Biology 195 (3): 687–700. doi:10.1016/0022-2836(87)90190-2.
- ↑ Li, Shuying; Wackett, Lawrence P. (1993). "Reductive dehalogenation by cytochrome P450CAM: Substrate binding and catalysis". Biochemistry 32 (36): 9355–9361. doi:10.1021/bi00087a014.
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| CYP1 | |
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| CYP2 | |
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| CYP3 (CYP3A) | |
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| CYP4 | |
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| CYP5-20 | |
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| CYP21-51 | |
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| CYP101-120 | |
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| CYP201-300 | |
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| CYP301-320 | |
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