Pyruvate Site of Pyruvate Phosphate Dikinase: Crystal Structure of the Enzyme

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Osnat Herzberg, Celia C. H. Chen, Sijiu Liu, Aleksandra Tempczyk, Andrew Howard, Min Wei, Dongmei Ye, and Debra Dunaway-Mariano
Biochemistry, December 19, 2001
10.1021/bi011799+ S0006-2960(02)05949-4
Copyright © 2001 American Chemical Society PPDK1 catalyzes the interconversion of ATP, Pi, and pyruvate, with AMP, PPi, and PEP, in three Mg2+-dependent partial reactions that involve phospho- and pyrophosphoenzyme intermediates. These reactions are reversible, and the outcome depends o­n the host organism (glycolytic ATP synthesis, or PEP synthesis). Enzyme phosphorylation and pyrophosphorylation occur o­n a histidine residue, His455. The nucleotide binding site is located within the N-terminal part of the polypeptide chain, whereas the pyruvate/PEP binding site is located within the C-terminal part of the chain.

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