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. 1986 Mar;5(3):475–481. doi: 10.1002/j.1460-2075.1986.tb04236.x

The structure of cat muscle pyruvate kinase.

H Muirhead, D A Clayden, D Barford, C G Lorimer, L A Fothergill-Gilmore, E Schiltz, W Schmitt
PMCID: PMC1166788  PMID: 3519210

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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Selected References

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