Structural highlights
Function
[CPXA_PSEPU] Involved in a camphor oxidation system.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
We have synthesized two luminescent probes (D-4-Ad and D-8-Ad) that target cytochrome P450cam. D-4-Ad luminescence is quenched by Forster energy transfer upon binding (Kd = 0.83 muM) but is restored when the probe is displaced from the active site by camphor. In contrast, D-8-Ad (Kd approximately 0.02 muM) is not displaced from the enzyme, even in the presence of a large excess of camphor. The 2.2 A resolution crystal structure of the D-8-Ad:P450cam complex reveals extensive hydrophobic contacts between the probe and the enzyme, which result from the conformational flexibility of the B', F, and G helices. Probes with properties similar to those of D-4-Ad potentially could be useful for screening P450 inhibitors.
Fluorescent probes for cytochrome p450 structural characterization and inhibitor screening.,Dunn AR, Hays AM, Goodin DB, Stout CD, Chiu R, Winkler JR, Gray HB J Am Chem Soc. 2002 Sep 4;124(35):10254-5. PMID:12197708[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dunn AR, Hays AM, Goodin DB, Stout CD, Chiu R, Winkler JR, Gray HB. Fluorescent probes for cytochrome p450 structural characterization and inhibitor screening. J Am Chem Soc. 2002 Sep 4;124(35):10254-5. PMID:12197708
