Bacterial cytochromes P‐450
- 1 June 1996
- journal article
- review article
- Published by Wiley in Molecular Microbiology
- Vol. 20 (6) , 1115-1125
- https://doi.org/10.1111/j.1365-2958.1996.tb02632.x
Abstract
Summary: The cytochromes P‐450 (P‐450s) constitute an extremely large family ('superfamily') of haemoproteins that catalyse the oxidation of a wide range of physiological and non‐physiological compounds. A remarkable feature of the P‐450s is the manipulation of the same basic structure and chemistry to achieve an enormous range of functions in organisms as diverse as bacteria and man. Indeed, the P‐450s have been described as ‘the most versatile biological catalyst known’. Much research is focussed on mammalian P‐450s, with their roles in such processes as steroid transformations and the metabolism of carcinogens and other xenobiotics. However, our knowledge of the structure and function of the P‐450s has been advanced by analysis of a limited number of its bacterial members, primarily P‐450cam from Pseudomonas putida. Four P‐450 structures have been solved to date, all of which are from bacterial sources. The aim of this review is to assess current knowledge of the many bacterial P‐450s, with emphasis on their diverse biological roles and on the advances in our knowledge of this extremely important enzyme class, which have been made feasible through their study.This publication has 61 references indexed in Scilit:
- High-resolution crystal structure of cytochrome P450camPublished by Elsevier ,2005
- The Role of Barbie Box Sequences as cis-Acting Elements Involved in the Barbiturate-mediated Induction of Cytochromes P450BM−1 and P450BM−3 in Bacillus megateriumPublished by Elsevier ,1995
- Nucleotide sequence of the gene encoding a repressor for the cytochrome P-450cam hydroxylase operon on the Pseudomonas putida CAM plasmidBiochimie, 1994
- Crystal structure and refinement of cytochrome P450terp at 2·3 Å resolutionJournal of Molecular Biology, 1994
- The P450 Superfamily: Update on New Sequences, Gene Mapping, Accession Numbers, Early Trivial Names of Enzymes, and NomenclatureDNA and Cell Biology, 1993
- Crystal structures of cytochrome P-450CAM complexed with camphane, thiocamphor, and adamantane: factors controlling P-450 substrate hydroxylationBiochemistry, 1991
- Ferredoxins from two sulfonylurea herbicide monooxygenase systems in Streptomyces griseolusBiochemistry, 1991
- Cytochrome P-450cam binding surface defined by site-directed mutagenesis and electrostatic modelingBiochemistry, 1990
- Induction by barbiturates of a cytochrome P-450-dependent fatty acid monooxygenase in Bacillus Megaterium: Relationship between barbiturate structure and inducer activityBiochemical and Biophysical Research Communications, 1983
- formation of 9,10-epoxypalmitate and 9,10-dihydroxypalmitate from palmitoleic acid by a soluble system from BacillusmegateriumBiochemical and Biophysical Research Communications, 1978