Bacterial cytochromes P-450
| Autor: | Andrew W. Munro, J. Gordon Lindsay |
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| Rok vydání: | 1996 |
| Předmět: |
Models
Molecular Bacteria biology SUPERFAMILY Computational biology biology.organism_classification Microbiology Pseudomonas putida Mixed Function Oxygenases Structure and function Evolution Molecular Bacterial Proteins Cytochrome P-450 Enzyme System Animals NADPH-Ferrihemoprotein Reductase Molecular Biology |
| Zdroj: | Molecular Microbiology. 20:1115-1125 |
| ISSN: | 1365-2958 0950-382X |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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