The structure and function of 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.

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The structure of cat muscle pyruvate kinase.

Muirhead¹,

Clayden²,

Barford³

et al. 1986

The EMBO Journal

255

193

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ATP-dependent phosphorylation of α-substituted carboxylic acids catalyzed by pyruvate kinase

Ash

Goodhart

Reed

1984

Archives of Biochemistry and Biophysics

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Characterization of pyruvate kinase isolated from the adductor muscle of the mollusc Scapharca inaequivalvis

Cortesi

Fabbri

Isani

et al. 1985

Comparative Biochemistry and Physiology Part B: Comparative Bio

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The structure and function of pyruvate kinase

Cited by 6 publications

References 3 publications

The structure of cat muscle pyruvate kinase.

The structure of cat muscle pyruvate kinase.

ATP-dependent phosphorylation of α-substituted carboxylic acids catalyzed by pyruvate kinase

Characterization of pyruvate kinase isolated from the adductor muscle of the mollusc Scapharca inaequivalvis

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