Adenosine deaminase

ADA
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesADA, entrez:100, Adenosine deaminase, ADA1
External IDsOMIM: 608958; MGI: 87916; HomoloGene: 37249; GeneCards: ADA; OMA:ADA - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_000022
NM_001322050
NM_001322051

NM_001272052
NM_007398

RefSeq (protein)

NP_000013
NP_001308979
NP_001308980

NP_001258981
NP_031424

Location (UCSC)Chr 20: 44.58 – 44.65 MbChr 2: 163.57 – 163.59 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse
Adenosine/AMP deaminase
crystal structure of plasmodium yoelii adenosine deaminase (py02076)
Identifiers
SymbolA_deaminase
PfamPF00962
Pfam clanCL0034
InterProIPR001365
PROSITEPDOC00419
SCOP21add / SCOPe / SUPFAM
CDDcd01320
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Adenosine deaminase (editase) domain
Identifiers
SymbolA_deamin
PfamPF02137
InterProIPR002466
PROSITEPDOC00419
SCOP21add / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Adenosine/AMP deaminase N-terminal
Identifiers
SymbolA_deaminase_N
PfamPF08451
InterProIPR013659
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000196839Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000017697Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Wilson DK, Rudolph FB, Quiocho FA (May 1991). "Atomic structure of adenosine deaminase complexed with a transition-state analog: understanding catalysis and immunodeficiency mutations". Science. 252 (5010): 1278–1284. Bibcode:1991Sci...252.1278W. doi:10.1126/science.1925539. PMID 1925539.
  6. ^ Cristalli G, Costanzi S, Lambertucci C, Lupidi G, Vittori S, Volpini R, Camaioni E (Mar 2001). "Adenosine deaminase: functional implications and different classes of inhibitors". Medicinal Research Reviews. 21 (2): 105–128. doi:10.1002/1098-1128(200103)21:2<105::AID-MED1002>3.0.CO;2-U. PMID 11223861. S2CID 24003578.