H. Iwahana, M. Itakura
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引用次数: 2

摘要

氨基磷酸核糖基转移酶(ATase)被认为是嘌呤核苷酸生物合成的调节变构酶。从15个不同的物种中克隆了ATase cdna和基因组dna。鸡、大鼠和人类ATase基因和AIRC(氨基咪唑核糖核苷酸羧化酶)基因紧密相连,并在0.2-0.6 kb的基因间区分化转录。测定了枯草芽孢杆菌ATase的晶体结构。ATase四聚体是一个甜甜圈形状的分子,每个ATase亚基组织在两个大小大致相等的结构域中。四个[4 Fe-4 S]簇位于四聚体的角上。ATase活性受PRPP的正调控,而受GMP和AMP的负调控。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
[Amidophosphoribosyltransferase].
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.
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