Iwahana H, Itakura M
Otsuka Department of Clinical and Molecular Nutrition, School of Medicine, University of Tokushima.
Nihon Rinsho. 1996 Dec;54(12):3202-6.
Amidophosphoribosyltransferase (ATase) is the supposed regulatory allosteric enzyme of de novo purine nucleotide biosynthesis. ATase cDNAs and genomic DNAs were cloned from 15 different species. The chicken, rat, and human ATase genes and AIRC (aminoimidazole ribonucleotide carboxylase) genes are closely linked and divergently transcribed from an intergenic regions of 0.2-0.6 kb. The crystal structure of B. subtilis ATase was determined. The ATase tetramer is a doughnut-shaped molecule and each ATase subunit is organized in two domains of approximately equal size. The four [4 Fe-4 S] clusters are located at the corners of the tetramer. The activity of ATase is regulated positively by PRPP and negatively by GMP and AMP.
氨甲酰磷酸核糖转移酶(ATase)被认为是嘌呤核苷酸从头合成的调节变构酶。从15个不同物种中克隆出了ATase的cDNA和基因组DNA。鸡、大鼠和人类的ATase基因与氨基咪唑核糖核苷酸羧化酶(AIRC)基因紧密相连,并从0.2 - 0.6 kb的基因间区域反向转录。确定了枯草芽孢杆菌ATase的晶体结构。ATase四聚体是一个甜甜圈形状的分子,每个ATase亚基由两个大小大致相等的结构域组成。四个[4Fe - 4S]簇位于四聚体的角上。ATase的活性受到PRPP的正向调节以及GMP和AMP的负向调节。