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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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The structure of cat muscle pyruvate kinase.

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.[1]

References

  1. The structure of cat muscle pyruvate kinase. Muirhead, H., Clayden, D.A., Barford, D., Lorimer, C.G., Fothergill-Gilmore, L.A., Schiltz, E., Schmitt, W. EMBO J. (1986) [Pubmed]
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