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The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families

Nature Structural Biology volume 3, pages 74–86 (1996)Cite this article

Abstract

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.

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Authors and Affiliations

  1. Department of Biological Sciences, Purdue University West Lafayette, Indiana, 47907, USA

    John J.G. Tesmer & Janet L. Smith

  2. Department of Medicinal Chemistry and Pharmacognosy, Purdue University West Lafayette, Indiana, 47907

    Thomas J. Klem, Michael L. Deras & V. Jo Davisson

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Tesmer, J., Klem, T., Deras, M. et al. The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families. Nat Struct Mol Biol 3, 74–86 (1996). https://doi.org/10.1038/nsb0196-74

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