Analysis of medaka cytochrome P450 3A homotropic and heterotropic cooperativity.

Published

Journal Article

We have previously demonstrated that medaka CYP3A is associated with metabolism of several endobiotics including steroids and bile acids. In this study, we demonstrate that medaka CYP3A catalysis exhibits unusual kinetic behaviors consistent with allosteric interaction which cannot be described by hyperbolic kinetic models. Using 7-benzyloxy-4-(trifluoromethyl)-coumarin (BFC) and nonylphenol as CYP3A substrates, we describe both homotropic and heterotropic cooperative interactions. Given the role of CYP3A in maintaining the homeostatic balance for numerous endobiotics, enzymatic activation/inhibition by endocrine disruptors (EDCs) represents a putative (non-genomic) mechanism for endocrine disruption.

Full Text

Duke Authors

Cited Authors

  • Kullman, SW; Kashiwada, S; Hinton, DE

Published Date

  • August 2004

Published In

Volume / Issue

  • 58 / 2-5

Start / End Page

  • 469 - 473

PubMed ID

  • 15178067

Pubmed Central ID

  • 15178067

Electronic International Standard Serial Number (EISSN)

  • 1879-0291

International Standard Serial Number (ISSN)

  • 0141-1136

Digital Object Identifier (DOI)

  • 10.1016/j.marenvres.2004.03.030

Language

  • eng