Biochemical and molecular genetic correlation in adenylosuccinate lyase deficiency.

C Salerno, C Crifò

Journal: Nucleosides, nucleotides & nucleic acids 2005;23(8-9):1253-5

PMID: 15571240

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.

Address: Department of Gynecology, Perinatology and Child Health, University of Roma La Sapienza, Roma, Italy.

DOI: 10.1081/NCN-200027513

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MeSH Terms: Adenylosuccinate Lyase, Aldehydes, Binding Sites, Catalysis, Crystallography, X-Ray, Cysteine, Disulfides, Humans, Kinetics, Oxidative Stress, Protein Structure, Tertiary