title: Bacterial pyruvate kinases have a shorter N-terminal domain.
abstract: The N-terminal portions of the two forms of pyruvate kinase (EC2.7.1.40) from Escherichia coli have been sequenced up the 48th and 43rd residue, respectively. Comparison with the known primary structures shows that bacterial enzymes lack a substantial portion of the N-terminal sequence with respect to pyruvate kinases from vertebrates. This makes the suggested functional role of the N-terminal domain unlikely [Muirhead, H. (1990) Biochem. Soc. Trans. 18, 193-196] although an elongation of this domain with evolution is apparent.
authors.affiliation: Dipartimento di Biochimica, Università di Pavia.
authors.forename: G
authors.initials: G
authors.lastname: Valentini
authors.forename: M
authors.initials: M
authors.lastname: Stoppini
authors.forename: M L
authors.initials: ML
authors.lastname: Speranza
authors.forename: M
authors.initials: M
authors.lastname: Malcovati
authors.forename: G
authors.initials: G
authors.lastname: Ferri
mesh_terms: D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000201:enzymology*; D007527:Isoenzymes / Q000737:chemistry; D008969:Molecular Sequence Data; D011770:Pyruvate Kinase / Q000737:chemistry*; D013149:Spiroplasma / Q000201:enzymology*
chemical_list: D007527:Isoenzymes; D011770:Pyruvate Kinase