Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structure

• DOI: 10.1128/jb.169.2.751-757.1987
• Publication Date: 2016-11-02T22:42:19Z
• Authors: A Ben-Bassat; K Bauer; S Y Chang; K Myambo; A Boosman; S Chang
• Keywords: Oligopeptidase

Methionine aminopeptidase (MAP) catalyzes the removal of amino-terminal methionine from proteins. The Escherichia coli map gene encoding this enzyme was cloned; it consists 264 codons and encodes a monomeric 29,333 daltons. In vitro analyses with purified indicated that MAP is metallo-oligopeptidase absolute specificity for methionine. residues end recombinant proteins interleukin-2 (Met-Ala-Pro-IL-2) ricin A (Met-Ile-Phe-ricin A) could be removed either in or vivo MAP-hyperproducing strains E. coli. substrate preference adjacent to initiation significantly influence cleavage process. This conclusion consistent, general, deduced based on analysis known sequences intracellular (S. Tsunasawa, J. W. Stewart, F. Sherman, Biol. Chem. 260:5382-5391, 1985).