Tesmer J J, Klem T J, Deras M L, Davisson V J, Smith J L
Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA.
Nat Struct Biol. 1996 Jan;3(1):74-86. doi: 10.1038/nsb0196-74.
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.
GMP合成酶的晶体结构是两类代谢酶的原型。GMP合成酶的I类谷氨酰胺酰胺转移酶结构域存在于嘌呤、嘧啶、色氨酸、精氨酸、组氨酸和叶酸生物合成途径的相关酶中。该结构域包括一个保守的半胱氨酸-组氨酸-谷氨酸三联体，代表了一类利用催化三联体进行酶促水解的新酶家族。GMP合成酶第二个结构域中核苷酸结合位点的结构和保守序列指纹与包括NAD合成酶、天冬酰胺合成酶和精氨琥珀酸合成酶在内的ATP焦磷酸酶家族相同。
