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. 1992 May 25;303(1):4-10.
doi: 10.1016/0014-5793(92)80465-s.

Cloning and characterization of the cDNA encoding human adenylosuccinate synthetase

S M Powell  1 , H Zalkin, J E Dixon
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Free article

Cloning and characterization of the cDNA encoding human adenylosuccinate synthetase

S M Powell et al. FEBS Lett. .
Free article

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, argininosuccinate synthetase (ASS), which catalyzes a chemically similar reaction. Both human liver and HeLa 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.

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