Two forms of pyruvate kinase in Escherichia coli. A comparison of chemical and molecular properties.
The two forms of pyruvate kinase (ATP:pyruvate 2-O-phosphotransferase, EC 2.7.1.40) present in Escherichia coli have been purified from the same cultures and crystallized. A modified procedure for the purification of type I pyruvate kinase is described. Molecular weight, subunit structure, amino acid composition, NH2-terminal amino acid, maps of tryptic peptides and conditions for crystallization have been determined for the two forms. A comparison of these data shows that the two forms are different proteins, each being a tetramer of identical subunits.
D000596:Amino Acids / Q000032:analysis; D003460:Crystallization; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology*; D046911:Macromolecular Substances; D008970:Molecular Weight; D011770:Pyruvate Kinase; D014357:Trypsin
D000596:Amino Acids; D046911:Macromolecular Substances; D011770:Pyruvate Kinase; D014357:Trypsin