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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.

May 2004 / Text revised.

PROSITE method (with tools and information) covered by this documentation:

A_DEAMINASE, PS00485; Adenosine and AMP deaminase signature  (PATTERN)

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

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00485 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00485 • Scan Swiss-Prot/TrEMBL entries against PS00485 • view ligand binding statistics

Matching PDB structures: 1A4L 1A4M 1ADD 1KRM ... [ALL]

1	Authors	Chang Z.Y., Nygaard P., Chinault A.C., Kellems R.E.
	Title	Deduced amino acid sequence of Escherichia coli adenosine deaminase reveals evolutionarily conserved amino acid residues: implications for catalytic function.
	Source	Biochemistry 30:2273-2280(1991).
	PubMed ID	1998686

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