CYP2C92

CYP2C92 is a member of the cytochrome P450 superfamily, within the 2C subfamily. It is predicted to encode a membrane-bound monooxygenase that participates in the oxidative metabolism of endogenous compounds and xenobiotics. As with other cytochrome P450 enzymes, CYP2C92 is presumed to be a heme-thiolate protein localized mainly to the endoplasmic reticulum and to contain the conserved motifs characteristic of the family, including the heme-binding sequence FxxGxCxG near the C-terminus.

Expression patterns reported for CYP2C92 in species where it has been identified suggest enrichment in hepatic tissue, with possible expression in other organs such as the intestine. Regulation of its expression, like that of other CYP2C enzymes, may involve nuclear receptors that respond to hormonal and xenobiotic signals, though specific regulatory mechanisms for CYP2C92 require further study.

Substrate specificity and catalytic activity for CYP2C92 are not well characterized in the available literature. Early in vitro data indicate a broad potential for metabolizing diverse substrates, but precise substrate lists, kinetics, and regioselectivity remain to be established through comprehensive functional assays and in vivo validation.

Genetic and clinical implications of CYP2C92 are not fully defined. Given the central role of CYP2C enzymes in drug metabolism, CYP2C92 could contribute to interindividual variability in pharmacokinetics if expressed in humans or other species of interest. Ongoing research and genome annotations are expected to clarify its evolutionary relationships, tissue distribution, and potential impact on pharmacology and toxicology.