Publications

• Purification and characterization of cytosolic pyruvate kinase from banana fruit.

  Turner W.L., Plaxton W.C.

  Cytosolic pyruvate kinase (PK(c)) from ripened banana (Musa cavendishii L.) fruits has been purified 543-fold to electrophoretic homogeneity and a final specific activity of 59.7 micromol of pyruvate produced/min per mg of protein. SDS/PAGE and gel-filtration FPLC of the final preparation indicate ... >> More

  Cytosolic pyruvate kinase (PK(c)) from ripened banana (Musa cavendishii L.) fruits has been purified 543-fold to electrophoretic homogeneity and a final specific activity of 59.7 micromol of pyruvate produced/min per mg of protein. SDS/PAGE and gel-filtration FPLC of the final preparation indicated that this enzyme exists as a 240 kDa homotetramer composed of subunits of 57 kDa. Although the enzyme displayed a pH optimum of 6.9, optimal efficiency in substrate utilization [in terms of V(max)/K(m) for phosphoenolpyruvate (PEP) or ADP] was equivalent at pH 6.9 and 7.5. PK(c) activity was absolutely dependent upon the presence of a bivalent and a univalent cation, with Mg(2+) and K(+) respectively fulfilling this requirement. Hyperbolic saturation kinetics were observed for the binding of PEP, ADP, Mg(2+) and K(+) (K(m) values of 0.098, 0.12, 0.27 and 0.91 mM respectively). Although the enzyme utilized UDP, IDP, GDP and CDP as alternative nucleotides, ADP was the preferred substrate. L-Glutamate and MgATP were the most effective inhibitors, whereas L-aspartate functioned as an activator by reversing the inhibition of PK(c) by L-glutamate. The allosteric features of banana PK(c) are compared with those of banana PEP carboxylase [Law and Plaxton (1995) Biochem. J. 307, 807-816]. A model is presented which highlights the roles of cytosolic pH, MgATP, L-glutamate and L-aspartate in the co-ordinate control of the PEP branchpoint in ripening bananas. << Less

  Biochem J 352:875-882(2000) [PubMed] [EuropePMC]

  This publication is cited by 3 other entries.

• Enzymic synthesis of guanosine and cytidine triphosphates: a note on the nucleotide specificity of the pyruvate phosphokinase reaction.

  STROMINGER J.L.

  Biochim Biophys Acta 16:616-618(1955) [PubMed] [EuropePMC]

  This publication is cited by 5 other entries.

• Fluorokinase and pyruvic kinase.

  TIETZ A., OCHOA S.

  Arch Biochem Biophys 78:477-493(1958) [PubMed] [EuropePMC]

  This publication is cited by 5 other entries.

• Enzymatic phosphorylation of adenosine and 2,6-diaminopurine riboside.

  KORNBERG A., PRICER W.E. Jr.

  J Biol Chem 193:481-495(1951) [PubMed] [EuropePMC]

  This publication is cited by 6 other entries.