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ADA2 isoform of adenosine deaminase from pleural fluid
Author(s) -
Andreasyan Nune A.,
Hairapetyan Hripsime L.,
Sargisova Yelizaveta G.,
Mardanyan Sona S.
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.11.109
Subject(s) - ehna , adenosine deaminase , deamination , adenosine , isozyme , amp deaminase , chemistry , biochemistry , gene isoform , enzyme , gene
Adenosine deaminase isoenzyme 2 (ADA2) was isolated from human pleural fluid for the first time. Molecular and kinetic properties were characterized. It was shown that the inhibitors of adenosine deaminase isoenzyme 1 (ADA1), adenosine, and erithro‐9‐(2‐hydroxy‐3‐nonyl)adenine (EHNA) derivatives are poor inhibitors of ADA2. Comparison of the interaction of ADA2 and ADA1 with adenosine and its derivative, 1‐deazaadenosine, indicates that the isoenzymes have similar active centers. The absence of ADA2 inhibition by EHNA is evidence of a difference of these active centers in a close environment. The possible role of Zn 2+ ions and the participation of acidic amino acids Glu and Asp in adenosine deamination catalyzed by ADA2 were shown.