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Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structure
Open accessAbstract
Methionine aminopeptidase (MAP) catalyzes the removal of amino-terminal methionine from proteins. The Escherichia coli map gene encoding this enzyme was cloned; it consists of 264 codons and encodes a monomeric enzyme of 29,333 daltons. In vitro analyses with purified enzyme indicated that MAP is a metallo-oligopeptidase with absolute specificity for the amino-terminal methionine. The methionine residues from the amino-terminal end of the recombinant proteins interleukin-2 (Met-Ala-Pro-IL-2) and ricin A (Met-Ile-Phe-ricin A) could be removed either in vitro with purified MAP enzyme or in vivo in MAP-hyperproducing strains of E. coli. In vitro analyses of the substrate preference of the E. coli MAP indicated that the residues adjacent to the initiation methionine could significantly influence the methionine cleavage process. This conclusion is consistent, in general, with the deduced specificity of the enzyme based on the analysis of known amino-terminal sequences of intracellular proteins (S. Tsunasawa, J. W. Stewart, and F. Sherman, J. Biol. Chem. 260:5382-5391, 1985).
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Cited by
Wilcox, D. E. (1996) · Chemical Reviews · doi:10.1021/cr950043b · Cited by 893
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Link, A. J., Robison, K., & Church, G. M. (1997) · ELECTROPHORESIS · doi:10.1002/elps.1150180807 · Cited by 342
THE F0F1-TYPE ATP SYNTHASES OF BACTERIA: Structure and Function of the F0 Complex
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Chen, H., Wang, R.-F., & Cerniglia, C. E. (2004) · Protein Expression and Purification · doi:10.1016/j.pep.2003.12.016 · Cited by 180
Metadata
- Authors
- Ben-Bassat, A., Bauer, K., Chang, S. Y., Myambo, K., Boosman, A., & Chang, S.
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 1987-02
- Volume
- 169
- Issue
- 2
- Pages
- 751-757
- ISSN
- 0021-9193 (ISSN-L)
- 1098-5530
- OpenAlex
- W2155894308
- Cited by
- 506
- References
- 0
- FWCI
- 13.22
- Type
- journal article
- Language
- en
- Open access
- green
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- Ben-Bassat, A., Bauer, K., Chang, S. Y., Myambo, K., Boosman, A., & Chang, S. (1987). Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structure. Journal of Bacteriology. https://doi.org/10.1128/jb.169.2.751-757.1987
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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