id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-306755-9q1mawfs	Rivière, Guillaume	Characterization of the first angiotensin-converting like enzyme in bacteria: Ancestor ACE is already active	2007-09-01		.txt	text/plain	5364	301	52	Interestingly, in silico databank analysis revealed that bacterial DNA sequences could encode putative ACE-like proteins, strikingly similar to vertebrates' enzymes. Interestingly, and though in silico evidence suggest the presence of a two-domain ACE-related protein in mosquitoes (Burnham et al., 2005) , all the cloned genes encode soluble, single active site enzymes (Tatei et al., 1995; Taylor et al., 1996; Wijffels et al., 1996) . The protein encoded by this gene, referred to as XcACE (Xanthomonas citri angiotensin-converting enzyme), is a 672 amino-acid protein. Key active site residues such as the zinc-binding motif, His 513 and Tyr 526 (tACE numbering) are conserved in XcACE and many other ACE-like enzymes. However, in line with the assay results, the non-conserved active site residues are neither identical to the C-or N-domain of human ACE, and are the presumed cause of the different substrate selectivity and inhibition profile of XcACE. Functional conservation of the active sites of human and Drosophila angiotensin I-converting enzyme	./cache/cord-306755-9q1mawfs.txt	./txt/cord-306755-9q1mawfs.txt