| First Author | Powell SM | Year | 1992 |
| Journal | FEBS Lett | Volume | 303 |
| Issue | 1 | Pages | 4-10 |
| PubMed ID | 1592113 | Mgi Jnum | J:42300 |
| Mgi Id | MGI:1095518 | Doi | 10.1016/0014-5793(92)80465-s |
| Citation | Powell SM, et al. (1992) Cloning and characterization of the cDNA encoding human adenylosuccinate synthetase. FEBS Lett 303(1):4-10 |
| abstractText | 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. |
