Crystal Structures of Staphylococcus aureus Methionine Aminopeptidase Complexed with Keto Heterocycle and Aminoketone Inhibitors Reveal the Formation of a Tetrahedral Intermediate-Reference-Cited by-同舟云学术

Crystal Structures of Staphylococcus aureus Methionine Aminopeptidase Complexed with Keto Heterocycle and Aminoketone Inhibitors Reveal the Formation of a Tetrahedral Intermediate

Published:2004-02-07 Issue:6 Volume:47 Page:1325-1328
ISSN:0022-2623
Container-title:Journal of Medicinal Chemistry
language:en
Short-container-title:J. Med. Chem.

Author:

Douangamath Alice¹,Dale Glenn E.¹,D'Arcy Allan¹,Almstetter Michael¹,Eckl Robert¹,Frutos-Hoener Annabelle¹,Henkel Bernd¹,Illgen Katrin¹,Nerdinger Sven¹,Schulz Henk¹,MacSweeney Aengus¹,Thormann Michael¹,Treml Andreas¹,Pierau Sabine¹,Wadman Sjoerd¹,Oefner Christian¹

Affiliation:

1. Morphochem AG, WRO-1055/388, Schwarzwaldallee 215, CH-4058 Basel, Switzerland

Publisher

American Chemical Society (ACS)

Subject

Drug Discovery,Molecular Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/jm034188j

Reference34 articles.

1. Control of protein life-span by N-terminal methionine excision

2. Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid.

3. The specificities of yeast methionine aminopeptidase and acetylation of amino-terminal methionine in vivo. Processing of altered iso-1-cytochromes c created by oligonucleotide transformation.

4. The NH2-terminal residues of the proteins from cell-free extracts of E. coli

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