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Kinetic properties of the common electrophoretic variants of human S‐adenosylhomocysteine hydrolase (AHCY): the effect of four nucleoside analogue inhibitors
Author(s) -
CORBO R. M.,
INGIANNA R.,
SCACCHP R.,
BOZZI A.
Publication year - 1992
Publication title -
annals of human genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.537
H-Index - 77
eISSN - 1469-1809
pISSN - 0003-4800
DOI - 10.1111/j.1469-1809.1992.tb01127.x
Subject(s) - adenosine , purine , nucleoside , chemistry , phenotype , biochemistry , riboside , microbiology and biotechnology , biology , stereochemistry , enzyme , gene
Summary Red blood cell S‐adenosylhomocysteine hydrolase (AHCY) from individuals of 1, 2‐1 and 3‐1 phenotypes was partially purified and K m and V max determined in the absence and in the presence of the following inhibitors: 3‐deaza‐adenosine (DZA), 3‐deaza‐aristeromycin (DZAry), 2–chloro adenosine (2‐Cl‐ado) and purine riboside (or nebularine). The three phenotypes 1, 2‐1, 3‐1 showed similar K m (32·58, 39·22 and 34·84 μ m respectively), but the ratio K m / V max was statistically different. DZA and DZAry appeared to be strong competitive inhibitors. The AHCY 1 phenotype was more resistant to their action, while the 3‐1 variant was more sensitive. 2‐Cl‐ado and purine riboside were weaker inhibitors; the type of inhibition varied among the three phenotypes, but, again, the AHCY 1 phenotype was less sensitive than the other two.