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Article

Single mutations change CYP2F3 from a dehydrogenase of 3-methylindole to an oxygenase.

Biochemistry - 16 Sept 2008

Kartha Jaya S, Skordos Konstantine W, Sun Hao, Hall Clifton, Easterwood LaHoma M, Reilly Christopher A, Johnson Eric F, Yost Garold S

Abstract excerpt

Pulmonary cytochrome P450 2F3 (CYP2F3) catalyzes the dehydrogenation of the pneumotoxin 3-methylindole (3MI) to an electrophilic intermediate, 3-methyleneindolenine, which is responsible for the toxicity of the parent compound. Members of the CYP2F subfamily are the only enzymes known to exclusively dehydrogenate 3MI, without detectable formation of oxygenation products. Thus, CYP2F3 is an attractive model to...

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Identifiers

PMID: 18717595
DOI: 10.1021/bi8005658
PMCID: PMC2843524

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