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phosphoenolpyruvate carboxykinase
Catalysis from A to Z, 2020F.‐S. Liang
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Phosphoenolpyruvate carboxykinase (ATP) [PDF]
, 1990 Margit Salzmann, Dietmar Schomburg
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Phosphoenolpyruvate carboxykinase: Structure, function and regulation
2002Abstract The aim of this article is to outline our understanding of the enzyme phosphoenolpyruvate carboxykinase (PEPCK). Although emphasis is placed on the enzyme derived from flowering plants, other organisms are also considered, because comparative studies provide invaluable information. The following points are considered in detail.
Robert P. Walker, Zhi-Hui Chen
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Phosphoenolpyruvate carboxykinase activity in Ascaris suum muscle
Comparative Biochemistry and Physiology, 1969Abstract 1. 1. Phosphoenolpyruvate (PEP) carboxykinase activity was measured for four subcellular fractions of Ascaris suum muslce. Mos activity was associated with the soluble fraction. 2. 2. The reaction had a pH optimum of about 7·2. 3. 3. Mn ++ was a more effective promoter of the reaction than Mg ++ . 4. 4.
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The Regulation of Phosphoenolpyruvate Carboxykinase in Fetal Rat Liver [PDF]
Enzyme and Protein, 1973 Lea Reshef +3 more
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Phosphoenolpyruvate Carboxykinase in the Developing Pig Liver
Neonatology, 1971M. Cornblath, K.R. Swiatek, J.T. Tildon
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Phosphoenolpyruvate carboxykinase (pyrophosphate)
1990Dietmar Schomburg, Margit Salzmann
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