Cytochromes P450: History, Classes, Catalytic Mechanism, and Industrial Application

Cook, D., Finnigan, J., Cook, K., Black, Gary and Charnock, S. J. (2016) Cytochromes P450: History, Classes, Catalytic Mechanism, and Industrial Application. In: Insights into Enzyme Mechanisms and Functions from Experimental and Computational Methods. Elsevier, London, pp. 105-126. ISBN 978-0-12-804825-2

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Official URL: http://dx.doi.org/10.1016/bs.apcsb.2016.07.003

Abstract

Cytochromes P450, a family of heme-containing monooxygenases that catalyze a diverse range of oxidative reactions, are so-called due to their maximum absorbance at 450 nm, ie, “Pigment–450 nm,” when bound to carbon monoxide. They have appeal both academically and commercially due to their high degree of regio- and stereoselectivity, for example, in the area of active pharmaceutical ingredient synthesis. Despite this potential, they often exhibit poor stability, low turnover numbers and typically require electron transport protein(s) for catalysis. P450 systems exist in a variety of functional domain architectures, organized into 10 classes. P450s are also divided into families, each of which is based solely on amino acid sequence homology. Their catalytic mechanism employs a very complex, multistep catalytic cycle involving a range of transient intermediates. Mutagenesis is a powerful tool for the development of improved biocatalysts and has been used extensively with the archetypal Class VIII P450, BM3, from Bacillus megaterium, but with the increasing scale of genomic sequencing, a huge resource is now available for the discovery of novel P450s.

Item Type: Book Section
Uncontrolled Keywords: 1α,25-Dihydroxyvitamin D3; (+)-Nootkatone; APIs; CYP; Ferredoxin; Flavodoxin; Flavoprotein; Hydroxylations; P450cam; Pravastatin; Protoporphyrin IX; Uncoupling
Subjects: C700 Molecular Biology, Biophysics and Biochemistry
Department: Faculties > Health and Life Sciences > School of Life Sciences > Applied Sciences
Depositing User: Becky Skoyles
Date Deposited: 01 Sep 2016 10:37
Last Modified: 10 Nov 2016 12:41
URI: http://nrl.northumbria.ac.uk/id/eprint/27641

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