The structure of cat muscle pyruvate kinase.
- 1 March 1986
- journal article
- research article
- Published by Springer Nature in The EMBO Journal
- Vol. 5 (3) , 475-481
- https://doi.org/10.1002/j.1460-2075.1986.tb04236.x
Abstract
The complete amino acid sequence of cat muscle pyruvate kinase has been determined and fitted to the 2.6 A resolution electron density map. Residues in the active site region are highly conserved in the cat muscle, chicken muscle, rat liver and yeast enzymes. The enzyme-bound magnesium, which is essential for activity, interacts with the side chain of glutamate-271 and with two main carbonyl groups. Lysine-269 is the probable acid/base catalyst responsible for the interconversion of pyruvate and enolpyruvate. A possible binding site for the essential monovalent cation is proposed.This publication has 26 references indexed in Scilit:
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