|PROSITE documentation PDOC00419
Adenosine and AMP deaminase signature
Adenosine deaminase (EC 126.96.36.199) catalyzes the hydrolytic deamination of
adenosine into inosine. AMP deaminase (EC 188.8.131.52) catalyzes the hydrolytic
deamination of AMP into IMP. It has been shown  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.
May 2004 / Text revised.
PROSITE method (with tools and information) covered by this documentation:
|A_DEAMINASE, PS00485; Adenosine and AMP deaminase signature (PATTERN)
The 2 D's may be active site residues
|Sequences known to belong to this class detected by the pattern:
|Other sequence(s) detected in Swiss-Prot:
|Matching PDB structures:
1A4L 1A4M 1ADD 1KRM ... [ALL]
||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.
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