Cloning and characterization of the cDNA encoding human adenylosuccinate synthetase.

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Powell SM, Zalkin H, Dixon JE

Cloning and characterization of the cDNA encoding human adenylosuccinate synthetase.

FEBS Lett. 1992 May 25;303(1):4-10.

PubMed ID

1592113 [ View in PubMed

]

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.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Aspartic acid	Adenylosuccinate Synthetases (Protein Group)	Protein group	Humans	Unknown	Substrate	Details

Polypeptides

Name	UniProt ID
Adenylosuccinate synthetase isozyme 2	P30520	Details