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Phosphorylation and Modulation of Enzymic Activity of 3-Hydroxy-3-Methylglutaryl Coenzyme A Reductase by Multiple Kinases

  • Zafarul H. Beg
  • John A. Stonik
  • H. Bryan BrewerJr.
Part of the GWUMC Department of Biochemistry Annual Spring Symposia book series (GWUN)

Abstract

3-Hydroxy-3-methylglutaryl coenzyme A reductase (HMG-CoA reductase, EC 1.1.1.34) is the rate-limiting enzyme which regulates the synthesis of cholesterol and other polyisoprenoid compounds (Rodwellet al., 1976; Goldstein and Brown, 1977; Brown and Goldstein, 1980; Ingebritsen and Gibson, 1980; Beg and Brewer, 1981, 1982; Kennelly and Rodwell, 1985; Beget al., 1987). In mammalian cells, HMG-CoA reductase is a transmembrane glycoprotein with its active site facing the cytosol and a carbohydrate-containing site oriented toward the luminal surface of the endoplasmic reticulum. The protomer of HMG-CoA reductase is an approximately 100,000-D protein (Chinet al., 1984). Proteolysis (Nesset al., 1981) of the native protein results in a 53,000 molecular weight fragment that contains the active site of the enzyme (Chinet al., 1984).

Keywords

Mevalonic Acid Molecular Weight Fragment Kinase System Phosphoprotein Phosphatase Methylglutaryl Coenzyme 
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

© Plenum Press, New York 1989

Authors and Affiliations

  • Zafarul H. Beg
    • 1
  • John A. Stonik
    • 1
  • H. Bryan BrewerJr.
    • 1
  1. 1.Molecular Disease Branch, National Heart, Lung, and Blood InstituteNational Institutes of HealthBethesdaUSA

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