Recombinant pyruvate kinase type I from Escherichia coli: Overproduction and revised C-terminus of the polypeptide

Biological Chemistry

Volumn 378, Issue 7, 1997, Pages 719-721

  Valentini, Giovanna ^a,b   Mattevi, Andrea ^a   Barilla', Daniela ^a,c   Galizzi, Alessandro ^a,b   Speranza, M Luisa ^a  

^a UNIVERSITY OF PAVIA   (Italy)

^b CISMI   (Italy)

^c UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

Cloning; Overexpression; Sequence

Indexed keywords

BACTERIAL ENZYME; PYRUVATE KINASE; RECOMBINANT PROTEIN; RNA POLYMERASE;

AMINO ACID SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL TRANSFORMATION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME PURIFICATION; ENZYME STRUCTURE; ESCHERICHIA COLI; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; STOP CODON;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BASE SEQUENCE; CLONING, MOLECULAR; ESCHERICHIA COLI; MOLECULAR SEQUENCE DATA; POLYMERASE CHAIN REACTION; PYRUVATE KINASE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0030877285     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (19)

1. Boiteux, A., Markus, M., Plesser, T., Hess, B., and Malcovati, M. (1983). Analysis of progress curves. Interaction of pyruvate kinase from Escherichia coli with fructose 1,6-bisphosphate and calcium ions. Biochem. J. 211, 631-640.
2. Bucher, T., and Pfeiderer, G. (1955). Pyruvate kinase from muscle. Methods Enzymol. 1, 435-440.
3. Fothergill-Gilmore, L.A., and Michels, P.A. (1992). Evolution of glycolysis. Progr. Mol. Biol. Biophys. 59, 105-227.
4. Glaser, P., Kunst, F., Arnaud, M., and Danchin, A. (1993). Bacillus subtilis genome project: cloning and sequencing of the 97 kb region from 325° to 333°. Mol. Microbiol. 10, 371-384.
5. 2+ and pyruvate. Biochemistry 33, 6301-6309.
6. Lowry, O.M., Rosebrough, M.J., Farr, A.L., and Randall, R.J. (1951). Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265-275.
7. Mattevi, A., Valentini, G., Rizzi, M., Speranza, M. L., Bolognesi, M., and Coda, A. (1995a). Crystal structure of Escherichia coli pyruvate kinase type I: molecular basis of the allosteric mechanism. Structure 3, 729-741.
8. Mattevi, A., Valentini, G., Speranza, M.L., Sartori, P., Bolognesi, M., and Coda, A. (1995b). Crystallization and preliminary X-ray analysis of pyruvate kinase type I from Escherichia coli. Acta Cryst. D51, 1089-1091.
9. Mattevi, A., Bolognesi, M., and Valentini, G. (1996). The allosteric regulation of pyruvate kinase. FEBS Lett. 389, 15-19.
10. Muirhead, H., Clayden, D.A., Barford, D., Lorimer, C.G., Fothergill-Gilmore, L.A., Schlitz, F., and Schmitt, W. (1986). Structure of cat muscle pyruvate kinase. EMBO J. 5, 475-481.
11. Ohara, O., Dorit, R.L., and Gilbert, W. (1989). Direct genomic sequencing of bacterial DNA: The pyruvate kinase I gene of Escherichia coli. Proc. Natl. Sci. USA 86, 6883-6887.
12. Ohara, O., Dorit, R.L., and Gilbert, W. (1990). GenBank accession number M 24636.
13. Sanger, F., Nicklen, S., and Consler, A.R. (1977). DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74, 5463-5467.
14. Speranza, M.L., Valentini, G., Iadarola, P., Stoppini, M., Malcovati, M., and Ferri, G. (1989). Primary structure of three peptides at the catalytic and allosteric sites of the fructose-1,6-bisphosphate-activated pyruvate kinase from Escherichia coli. Biol. Chem. Hoppe-Seyler 370, 211-216.
15. Speranza, M.L., Valentini, G., and Malcovati, M. (1990). Fructose-1,6-bisphosphate-activated pyruvate kinase from Escherichia coli: nature of bonds involved in the allosteric mechanism. Eur. J. Biochem. 191, 701-704.
16. Speranza, M.L., Valentini, G., Ferri, G., and Malcovati, M. (1992). Fructose-1,6-phosphate-activated pyruvate kinase from Escherichia coli: ligand-promoted conformational changes. Ital. J. Biochem. 41, 200-211.
17. Studier, W., Rosenberg, A.H., Dunn, J.J., and Dubendorff, J.W. (1990). Use of a T7 RNA polymerase to direct expression of cloned genes. Methods Enzymol. 185, 60-89.
18. Valentini, G., Iadarola, P., Ferri, G., and Speranza, M.L. (1995). Affinity labelling of the catalytic and allosteric ATP binding sites of pyruvate kinase type I from Escherichia coli. Biol. Chem. Hoppe-Seyler 376, 231-235.
19. Waigood, E. B., and Sanwal, B. O. (1974). The control of pyruvate kinase of Escherichia coli. Physicochemical and regulatory properties of the enzyme activated by fructose 1,6-diphosphate. J. Biol. Chem. 249, 265-274.