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Two forms of pyruvate kinase in Escherichia coli. a comparison of chemical and molecular properties

Valentini, G.; Iadarola, P.; Somani, B.L.; Malcovati, M.

Biochimica et Biophysica Acta 570(2): 248-258

1979

ISSN/ISBN: 0006-3002
PMID: 387087
DOI: 10.1016/0005-2744(79)90145-1
Accession: 041878649
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.

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Related References

Valentini, G.; Iadarola, P.; Somani, B.L.; Malcovati, M. 1979: 2 forms of pyruvate kinase ec 2.7.1.40 in escherichia coli a comparison of chemical and molecular properties Biochimica et Biophysica Acta 70(2): 248-258
Tanaka, K.; Sakai, H.; Ohta, T.; Matsuzawa, H. 1995: Molecular cloning of the genes for pyruvate kinase of two bacilli, Bacillus psychrophilus and Bacillus licheniformis, and comparison of the properties of the enzymes produced in Escherichia coli Bioscience Biotechnology and Biochemistry 59(8): 1536-1542
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