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The structure of cat muscle pyruvate kinase.
Authors:H Muirhead   D A Clayden   D Barford   C G Lorimer   L A Fothergill-Gilmore   E Schiltz     W Schmitt
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.
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