Cloning and characterization of the cDNA encoding human adenylosuccinate synthetase
- 25 May 1992
- journal article
- Published by Wiley in FEBS Letters
- Vol. 303 (1) , 4-10
- https://doi.org/10.1016/0014-5793(92)80465-s
Abstract
Adenylosuccinate synthetase (AS) catalyzes the first committed step in the conversion of IMP to AMP. A cDNA was isolated from a human liver library which encodes a protein of 455 amino acids (M r of 49.925). Alignments of human, mouse, Dictyostelium discoideum and E. coli AS sequences identify a number of invariant residues which are likely to be important for structure and/or catalysis. The human AS sequence was also 19% identical to the human urea cycle enzyme, arginosuccinate synthetase (ASS), which catalyses a chemically similar reaction. Both human liver and HcLa AS mRNA showed signals of 2.3 and 2.8 kb. An unmodified N‐terminus is required for function of the human AS enzyme in E. coli mutants lacking the bacterial enzyme. The human cDNA provides a means to assess the possible role of AS abnormalities in unclassified, idiopathic cases of gout.Keywords
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