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.
Biochemical and molecular genetic correlation in adenylosuccinate lyase deficiency / Salerno, Costantino; Crifo', Carlo. - In: NUCLEOSIDES, NUCLEOTIDES & NUCLEIC ACIDS. - ISSN 1525-7770. - STAMPA. - 23:(2004), pp. 1253-1255. [10.1081/NCN-200027513]
Biochemical and molecular genetic correlation in adenylosuccinate lyase deficiency
SALERNO, Costantino;CRIFO', Carlo
2004
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.