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130802s1995 xxu| s |||| 0|eng d |
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|a 9781475723915
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|a 10.1007/978-1-4757-2391-5
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|a (DE-He213)978-1-4757-2391-5
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|a Cytochrome P450
|h [electronic resource] :
|b Structure, Mechanism, and Biochemistry /
|c edited by Paul R. Ortiz de Montellano.
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| 250 |
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|a 2nd ed. 1995.
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| 264 |
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|a New York, NY :
|b Springer US :
|b Imprint: Springer,
|c 1995.
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| 300 |
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|a XII, 652 p.
|b online resource.
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| 336 |
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|a text
|b txt
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|a Springer eBook Collection
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|a I. Model Systems -- 1. Models and Mechanisms of Cytochrome P450 Action -- 2. Comparison of the Peroxidase Activity of Hemoproteins and Cytochrome P450 -- II. Structurally Defined Bacterial Enzymes -- 3. Twenty-five Years of P450camResearch: Mechanistic Insights into Oxygenase Catalysis -- 4. Structural Studies on Prokaryotic Cytochromes P450 -- 5. Bacterial P450s: Structural Similarities and Functional Differences -- III. Structures and Mechanisms of Membrane-Bound P450 Enzymes -- 6. Structures of Eukaryotic Cytochrome P450 Enzymes -- 7. NADPH Cytochrome P450 Reductase and Its Structural and Functional Domains -- 8. Oxygen Activation and Reactivity -- 9. Inhibition of Cytochrome P450 Enzymes -- IV Regulatory Mechanisms and Physiological Roles of Cytochrome P450 -- 10. Induction of Cytochrome P450 Enzymes that Metabolize Xenobiotics -- 11. Hormonal Regulation of Liver Cytochrome P450 Enzymes -- 12. Regulation of Steroidogenic and Related P450s -- 13. Cytochrome P450 and the Metabolism of Arachidonic Acid and Oxygenated Eicosanoids -- 14. Human Cytochrome P450 Enzymes -- 15. Heme—Thiolate Proteins Different from Cytochromes P450 Catalyzing Monooxygenations -- Appendices -- A. Cytochrome P450 Nomenclature and Alignment of Selected Sequences -- B. Rat and Human Liver Cytochromes P450: Substrate and Inhibitor Specificities and Functional Markers.
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| 520 |
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|a In the ten years that have elapsed since the first edition of this book went to press, the cytochrome P450 field has completed the transition to a discipline in which structure and mechanism, even regulation and biological function, are dealt with in molecular terms. The twin forces that have propelled this remarkable progress have been the widespread adoption of molecular biological approaches and the successful application of modem structural techniques. Only a few P450 primary sequences were available in 1985, whereas hundreds of P450 sequences are now available. Site-specific mutagenesis was then mostly a proverbial gleam in the eye of the P450 community, but it is now a standard technique in the research repertoire. The first crystal structure of a cytochrome P450 enzyme had just been solved in 1985 and appeared on the cover of the first edition. Today, the high-reso lution crystal structures of four soluble bacterial P450 enzymes are available and the race is on to develop approaches that will permit us to determine the structures of the membrane-bound forms of the enzyme. The past ten years has seen phenomenal progress let us hope that the next ten will prove equally exciting. The book is informally divided into four sections. In order to hold the book close to the advancing front of research, some of the chapter topics from the first edition have been dropped to make room for new or expanded topics.
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| 590 |
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|a Loaded electronically.
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| 590 |
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|a Electronic access restricted to members of the Holy Cross Community.
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| 650 |
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|a Pharmacology.
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| 650 |
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|a Biochemistry.
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| 690 |
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|a Electronic resources (E-books)
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| 700 |
1 |
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|a Ortiz de Montellano, Paul R.
|e editor.
|4 edt
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| 710 |
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