Crystal structure of Saccharomyces cerevisiae glutamine synthetase Gln1 suggests a nanotube-like supramolecular assembly
Crystal structure of Saccharomyces cerevisiae glutamine synthetase Gln1 suggests a nanotube-like supramolecular assembly
复制标题
酿酒酵母谷氨酰胺合成酶 Gln1 的晶体结构表明纳米管状超分子组装体
DOI:
10.1002/prot.22403
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发表时间:
2009-07-01
影响因子:
2.9
通讯作者:
Zhou, Cong-Zhao
中科院分区:
文献类型:
--
作者:
He, Yong-Xing;Gui, Long;Zhou, Cong-Zhao
Glutamine synthetase (GS, EC 6.3. 1.2) is an enzyme that catalyzes the condensation of glutamate and ammonium to form glutamine, with concomitant hydrolysis of ATP. 1 There are three different classes of GS enzymes, referred to as GSI, GSII, and GSIII. GSI enzymes are specific to prokaryotes and form oligomers of 12 identical subunits. 2 The activity of GSI enzyme is regulated by the adenylation of a tyrosine residue. 3 GSII enzymes are found in eukaryotes and some bacteria (Rhizobiaceae, Frankiaceae, and Streptomycetaceae families, which also have GSI). They form decamers of identical subunits. 4 In mammals, GSII enzymes eliminate free ammonia and convert the excitotoxic glutamate into glutamine, which is not neurotoxic. 5 In plants, there are two or more isoenzymes of GSII, which are targets of some herbicides because of their roles in ammonia assimilation. GSIII enzymes were first found in Bacteroides fragilis and identified afterward in a few more anaerobic bacteria and cyanobacteria. 6–8 They are hexamers of identical subunits which are much larger (about 700 residues) than that of GSI (450–470 residues) or GSII (350–420 residues) enzymes. 9