id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-264316-do0px1gq	Mucha, Artur	Metallo-aminopeptidase inhibitors	2010-05-10		.txt	text/plain	14674	769	41	This review focuses on the strict metallo-aminopeptidases because they constitute the largest and the most homogenous class of these enzymes and use one or two metal ions in their active sites to specifically release the N-terminal amino acid residues of polypeptides and proteins. Similar to other amino acid and peptide mimetics used as protease inhibitors, this is the effect of the incorporation of a covalent or non-covalent binding group (here involved in coordination of a catalytic metal ion(s) in the enzyme active site) into a substrate structure. Additionally, the P1 side chain of the aminophosphonic acid analogues (or more effectively, both P1 and P1 0 residues of the pseudopeptides phosphoryl moiety) gives further possibility of structural optimization of substituents interacting with the S1 and S1 0 binding pockets of the enzyme (Fig. 3) Fig. 4 ), appeared to be efficient inhibitors of LAP with a K i ¼ 0.15 [90] and 0.23 mM [87] for the R (L) enantiomers.	./cache/cord-264316-do0px1gq.txt	./txt/cord-264316-do0px1gq.txt