1gpm

Publication Abstract from PubMed

The crystal structure of GMP synthetase serves as a prototype for two families of metabolic enzymes. The Class I glutamine amidotransferase domain of GMP synthetase is found in related enzymes of the purine, pyrimidine, tryptophan, arginine, histidine and folic acid biosynthetic pathways. This domain includes a conserved Cys-His-Glu triad and is representative of a new family of enzymes that use a catalytic triad for enzymatic hydrolysis. The structure and conserved sequence fingerprint of the nucleotide-binding site in a second domain of GMP synthetase are common to a family of ATP pyrophosphatases, including NAD synthetase, asparagine synthetase and argininosuccinate synthetase.

The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families.,Tesmer JJ, Klem TJ, Deras ML, Davisson VJ, Smith JL Nat Struct Biol. 1996 Jan;3(1):74-86. PMID:8548458^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.