{PDOC00419} {PS00485; A_DEAMINASE} {BEGIN} ***************************************** * Adenosine and AMP deaminase signature * ***************************************** Adenosine deaminase (EC 3.5.4.4) catalyzes the hydrolytic deamination of adenosine into inosine. AMP deaminase (EC 3.5.4.6) catalyzes the hydrolytic deamination of AMP into IMP. It has been shown [1] that these two types of enzymes share three regions of sequence similarities; these regions are centered on residues which are proposed to play an important role in the catalytic mechanism of these two enzymes. We have selected one of these regions, it contains two conserved aspartic acid residues that are potential active site residues. -Consensus pattern: [SA]-[LIVM]-[NGS]-[STA]-D-D-P [The 2 D's may be active site residues] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: 3. -Last update: May 2004 / Text revised. [ 1] Chang Z.Y., Nygaard P., Chinault A.C., Kellems R.E. "Deduced amino acid sequence of Escherichia coli adenosine deaminase reveals evolutionarily conserved amino acid residues: implications for catalytic function." Biochemistry 30:2273-2280(1991). PubMed=1998686 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}