Bacterial pyruvate kinases have a shorter N-terminal domain

Biol Chem Hoppe Seyler. 1991 Feb;372(2):91-3. doi: 10.1515/bchm3.1991.372.1.91.

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Escherichia coli / enzymology*
  • Isoenzymes / chemistry
  • Molecular Sequence Data
  • Pyruvate Kinase / chemistry*
  • Spiroplasma / enzymology*

Substances

  • Isoenzymes
  • Pyruvate Kinase