Desensitization to glucose 6-phosphate of phosphoenolpyruvate carboxylase from maize leaves by pyridoxal 5′-phosphate
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference34 articles.
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1. Structural and biochemical evidence of the glucose 6-phosphate-allosteric site of maize C4-phosphoenolpyruvate carboxylase: its importance in the overall enzyme kinetics;Biochemical Journal;2020-06-12
2. Identification of the allosteric site for neutral amino acids in the maize C4 isozyme of phosphoenolpyruvate carboxylase: The critical role of Ser-100;Journal of Biological Chemistry;2018-06
3. The molecular binding interactions of inhibitors and activators of phosphoenolpyruvate carboxylase;Journal of Molecular Structure: THEOCHEM;2005-11
4. Influence of allosteric effectors on the kinetics and equilibrium binding of phosphoenolpyruvate (PEP) to phosphoenolpyruvate carboxylase (PEPC) from Zea mays;Biophysical Chemistry;2001-09
5. Kinetics of phosphoenolpyruvate carboxylase from Zea mays leaves at high concentration of substrates;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;2001-03
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