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Cytochrome P-450 Enzymes in Sterol Biosynthesis and Metabolism

  • Colin R. Jefcoate

Abstract

The biosynthesis of sterols involves a series of both simple and complex cytochrome P-450-catalyzed monooxygenase reactions. These processes are generally distinguished from the multiplicity of reactions catalyzed by hepatic microsomal forms of P-450 by involving P-450 isozymes that exhibit a high degree of regio- and stereospecificity. The cell specificity of these monooxygenases has been noted in the previous chapter. In this chapter, we will examine the biochemical control of these steroidogenic cytochromes P-450. This is far more stringent than for the hepatic cytochromes P-450 because of the physiological importance of steroid hormones and bile acids. While the biosynthesis of these cytochromes is under hormonal control, this response takes a minimum of 12 hr for steroidogenic cytochromes P-450 (see Chapter 10). More common fluctuations in activity are required within minutes or hours. Here we will discuss the mechanisms of steroid hydroxylation and also some of the proposed mechanisms for rapid physiological control of steroidogenic enzymes.

Keywords

Bile Acid Bile Acid Synthesis Sterol Biosynthesis Sterol Carrier Protein2 Kidney Mitochondrion 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1986

Authors and Affiliations

  • Colin R. Jefcoate
    • 1
  1. 1.Department of PharmacologyUniversity of Wisconsin Medical SchoolMadisonUSA

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