Template:STRUCTURE 4i4h

Crystal structure of CYP3A4 ligated to pyridine-substituted desoxyritonavirCrystal structure of CYP3A4 ligated to pyridine-substituted desoxyritonavir

Template:ABSTRACT PUBMED 23586711

FunctionFunction

[CP3A4_HUMAN] Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It performs a variety of oxidation reactions (e.g. caffeine 8-oxidation, omeprazole sulphoxidation, midazolam 1'-hydroxylation and midazolam 4-hydroxylation) of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Acts as a 1,8-cineole 2-exo-monooxygenase. The enzyme also hydroxylates etoposide.[1]

About this StructureAbout this Structure

4i4h is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  1. Sevrioukova IF, Poulos TL. Pyridine-Substituted Desoxyritonavir Is a More Potent Inhibitor of Cytochrome P450 3A4 than Ritonavir. J Med Chem. 2013 Apr 26. PMID:23586711 doi:10.1021/jm400288z
  1. Miyazawa M, Shindo M, Shimada T. Oxidation of 1,8-cineole, the monoterpene cyclic ether originated from eucalyptus polybractea, by cytochrome P450 3A enzymes in rat and human liver microsomes. Drug Metab Dispos. 2001 Feb;29(2):200-5. PMID:11159812

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA