Adenosine deaminase
From Proteopedia
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'''Adenosine deaminase''' (ADA) or '''double-stranded RNA-specific editase''' deaminates adenosine and deoxyadenosine into inosine or deoxyinosine. ADA is part of the purine metabolism. In humans ADA is involved in the development and maintenance of the immune system. ADA binds dipeptidyl peptidase IV. The complex acts as a positive regulator of T-cell coactivation and regulates lymphocytes-epithelial adhesion.<ref>PMID:1925539</ref> | '''Adenosine deaminase''' (ADA) or '''double-stranded RNA-specific editase''' deaminates adenosine and deoxyadenosine into inosine or deoxyinosine. ADA is part of the purine metabolism. In humans ADA is involved in the development and maintenance of the immune system. ADA binds dipeptidyl peptidase IV. The complex acts as a positive regulator of T-cell coactivation and regulates lymphocytes-epithelial adhesion.<ref>PMID:1925539</ref> | ||
| + | *'''Double-stranded RNA-specofoc adenosine deaminase''' catalyses the C-6 deamination of adenosine in viral RNAs and cellular pre-mRNA<ref>PMID:9735305</ref>. | ||
== Disease == | == Disease == | ||
Revision as of 08:56, 21 May 2024
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References
- ↑ Wilson DK, Rudolph FB, Quiocho FA. Atomic structure of adenosine deaminase complexed with a transition-state analog: understanding catalysis and immunodeficiency mutations. Science. 1991 May 31;252(5010):1278-84. PMID:1925539
- ↑ Liu Y, Herbert A, Rich A, Samuel CE. Double-stranded RNA-specific adenosine deaminase: nucleic acid binding properties. Methods. 1998 Jul;15(3):199-205. PMID:9735305 doi:10.1006/meth.1998.0624
- ↑ Larson ET, Deng W, Krumm BE, Napuli A, Mueller N, Van Voorhis WC, Buckner FS, Fan E, Lauricella A, DeTitta G, Luft J, Zucker F, Hol WG, Verlinde CL, Merritt EA. Structures of substrate- and inhibitor-bound adenosine deaminase from a human malaria parasite show a dramatic conformational change and shed light on drug selectivity. J Mol Biol. 2008 Sep 12;381(4):975-88. Epub 2008 Jun 24. PMID:18602399 doi:http://dx.doi.org/10.1016/j.jmb.2008.06.048
