Biol. Chcm. Hoppc-Seyler Vol. 374, pp. 69-74, January 1993 Giovanna VALENTINI", Monica STOPPINI", Paolo IADAROLA U , Massimo MALCOVATib, Giuseppina FERRI" and M. PERANZA a a b Dipartimentodi Biochimica. Univcrsita di Pavia. and Dipartimento di Biologia c Genetica per Ic Scicnze mcdiche. Unjversita di Milano (Received 23 September 1992) Summary: Pyridoxal 5'-phosphate incorporation into pyruvate kinase II from E. coli was decreased by the substrate phosphoeno/pyruvate and increased by the allosteric activator ribose 5-phosphate, the total incorporation being linearly related to inactivation. Four lysyl residues were substantially modified, whatever the incubation conditions were while two additional residues became reactive only in the presence of the allosteric activator. Six tryptic peptides containKcy terms: Pyruvate kinase, binding sites, E. coli. ing modified lysines were purified and sequenced. They defined five regions of pyruvate kinase II, since one of them contained two labelled lysines and included a peptide which also appeared independently. Sequence comparison with E. coli type I, yeast and cat muscle pyruvate kinases shows that the binding regions of pyruvate kinase II are clearly divergent from those of pyruvate kinase I and of the eukaryotic enzymes. Pyruvate kinase (EC 18.104.22.168), an important glycolytic enzyme, is a tetramer of identical
Biological Chemistry Hoppe-Seyler – de Gruyter
Published: Jan 1, 1993
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