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. 1992 Nov;100(3):1411–1416. doi: 10.1104/pp.100.3.1411

Metabolite Activation of Crassulacean Acid Metabolism and C4 Phosphoenolpyruvate Carboxylase 1

Vahe Bandarian 1, William J Poehner 1, Scott D Grover 1
PMCID: PMC1075800  PMID: 16653139

Abstract

The effects of glycine, alanine, serine, and various phosphorylated metabolites on the activity of phosphoenolpyruvate (PEP) carboxylase from Zea mays and Crassula argentea were studied. The maize enzyme was found to be activated by amino acids at a site that is separate from the glucose 6-phosphate binding site. The combination of glycine and glucose 6-phosphate synergistically reduced the apparent Km of the enzyme for PEP and increased the apparent Vmax. Of the amino acids tested, glycine showed the lowest apparent Ka and caused the greatest activation. d-Isomers of alanine and serine were more effective activators than the l-isomers. Unlike the maize enzyme, the Crassula enzyme was not activated by amino acids. Activation of either the Crassula or maize enzyme by glucose 6-phosphate occurred without dephosphorylation of the activator molecule. Furthermore, the Crassula enzyme was activated by two compounds containing phosphonate groups whose carbon-phosphorus bonds were not cleaved by the enzyme. A study of analogs of glucose 6-phosphate with Crassula PEP carboxylase revealed that the identity of the ring heteroatom was a significant structural feature affecting activation. Activation was not highly sensitive to the orientation of the hydroxyl group at the second or fourth carbon positions or to the presence of a hydroxyl group at the second position. However, the position of the phosphate group was found to be a significant factor.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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