Your browser version may not work well with NCBI's Web applications. More information here...
1: FEBS Lett. 1992 May 25;303(1):4-10.Click here to read Links

Cloning and characterization of the cDNA encoding human adenylosuccinate synthetase.

Powell SM, Zalkin H, Dixon JE.

Department of Biochemistry, Purdue University, West Lafayette, IN 49707.

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.

PMID: 1592113 [PubMed - indexed for MEDLINE]