Adenosine/AMP deaminase | |||||||||
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![]() crystal structure of plasmodium yoelii adenosine deaminase (py02076) | |||||||||
Identifiers | |||||||||
Symbol | A_deaminase | ||||||||
Pfam | PF00962 | ||||||||
Pfam clan | CL0034 | ||||||||
InterPro | IPR001365 | ||||||||
PROSITE | PDOC00419 | ||||||||
SCOP2 | 1add / SCOPe / SUPFAM | ||||||||
CDD | cd01320 | ||||||||
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Adenosine deaminase (editase) domain | |||||||||
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Identifiers | |||||||||
Symbol | A_deamin | ||||||||
Pfam | PF02137 | ||||||||
InterPro | IPR002466 | ||||||||
PROSITE | PDOC00419 | ||||||||
SCOP2 | 1add / SCOPe / SUPFAM | ||||||||
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Adenosine/AMP deaminase N-terminal | |||||||||
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Identifiers | |||||||||
Symbol | A_deaminase_N | ||||||||
Pfam | PF08451 | ||||||||
InterPro | IPR013659 | ||||||||
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Adenosine deaminase (also known as adenosine aminohydrolase, or ADA) is an enzyme (EC 3.5.4.4) involved in purine metabolism. It is needed for the breakdown of adenosine from food and for the turnover of nucleic acids in tissues.
Its primary function in humans is the development and maintenance of the immune system.[5] However, the full physiological role of ADA is not yet completely understood.[6]
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