Structural highlights
Function
[AMPM_STAA1] Removes the N-terminal methionine from nascent proteins (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
High-resolution crystal structures of Staphylococcus aureus methionine aminopeptidase I in complex with various keto heterocycles and aminoketones were determined, and the intermolecular ligand interactions with the enzyme are reported. The compounds are effective inhibitors of the S. aureus enzyme because of the formation of an uncleavable tetrahedral intermediate upon binding. The electron densities unequivocally show the enzyme-catalyzed transition-state analogue mimicking that for amide bond hydrolysis of substrates.
Crystal structures of Staphylococcusaureus methionine aminopeptidase complexed with keto heterocycle and aminoketone inhibitors reveal the formation of a tetrahedral intermediate.,Douangamath A, Dale GE, D'Arcy A, Almstetter M, Eckl R, Frutos-Hoener A, Henkel B, Illgen K, Nerdinger S, Schulz H, Mac Sweeney A, Thormann M, Treml A, Pierau S, Wadman S, Oefner C J Med Chem. 2004 Mar 11;47(6):1325-8. PMID:14998322[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Douangamath A, Dale GE, D'Arcy A, Almstetter M, Eckl R, Frutos-Hoener A, Henkel B, Illgen K, Nerdinger S, Schulz H, Mac Sweeney A, Thormann M, Treml A, Pierau S, Wadman S, Oefner C. Crystal structures of Staphylococcusaureus methionine aminopeptidase complexed with keto heterocycle and aminoketone inhibitors reveal the formation of a tetrahedral intermediate. J Med Chem. 2004 Mar 11;47(6):1325-8. PMID:14998322 doi:http://dx.doi.org/10.1021/jm034188j
