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Glucose-6-phosphatase

  • Robert C. Nordlie
  • Roger A. Jorgenson

Abstract

Glucose-6-phosphatase (D-glucose-6-phosphate phosphohydrolase; EG 3.1.3.9) is unique among gluconeogenic enzymes in a variety of respects. Not only is the enzyme either a part of, or extremely tightly bound to, membranes of the endoplasmic reticulum (Ernster et al., 1962) and nucleus (Gunderson and Nordlie, 1973, 1975), but it also manifests a multiplicity of functions including the synthesis of glucose-6-P* at rates which may equal or actually exceed that of glucose-6-P hydrolysis (Lueck et al., 1972). And intimate, activity-discriminant interrelationships exist between catalytic characteristics of the enzyme and the origin, nature, and physical state of the biomembranes with which it is associated.

Keywords

Nuclear Membrane Smooth Endoplasmic Reticulum Microsomal Preparation Catalytic Characteristic Inorganic Pyrophosphatase 
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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© Plenum Press, New York 1976

Authors and Affiliations

  • Robert C. Nordlie
    • 1
  • Roger A. Jorgenson
    • 1
  1. 1.Department of BiochemistryUniversity of North Dakota Medical SchoolGrand ForksUSA

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