Abstract
An homology model of human adenylosuccinate lyase structure shows that P100A substitution distorts the amino acid chain of domain I in the proximity of His‐86, which behaves as general acid in the catalysis, and may expose Cys‐98 and Cys‐99 to oxidising agents. This model is in line with the observation that the defective protein is strongly inhibited by 4‐hydroxy‐2‐nonenal, an hydroxyalkenal that is known to form thio‐ether linkage with proteins.
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