Peters J M, Dalrymple B P, Jorgensen W K
Commonwealth Scientific and Industrial Research Organisation, Division of Tropical Animal Production, Indooroopilly, Qld., Australia.
Biochem Biophys Res Commun. 1992 Feb 14;182(3):1040-6. doi: 10.1016/0006-291x(92)91836-f.
The complete nucleotide sequence of a putative glutathione synthetase gene (gsh II) has been determined from Anaplasma centrale. The predicted 308 amino acid protein has a molecular weight of 34,222 and is 32% identical to the enzyme, glutathione synthetase (EC 6.3.2.3), encoded by Escherichia coli gsh II. The previously proposed ATP-binding site is not highly conserved. The putative glutathione synthetase gene (gsh II) is preceded by an unassigned open reading frame. Downstream of gsh II is the 5' region of an open reading frame encoding a protein with significant similarity to bacterial D-alanine:D-alanine ligases (ADP forming) (EC 6.3.2.4). The predicted partial amino acid sequence is 33% identical to the amino acid sequence of the protein encoded by the E. coli ddl gene.
已从中央无形体中确定了一个假定的谷胱甘肽合成酶基因（gsh II）的完整核苷酸序列。预测的308个氨基酸的蛋白质分子量为34222，与由大肠杆菌gsh II编码的谷胱甘肽合成酶（EC 6.3.2.3）有32%的同源性。先前提出的ATP结合位点并非高度保守。假定的谷胱甘肽合成酶基因（gsh II）之前有一个未指定的开放阅读框。gsh II的下游是一个开放阅读框的5'区域，该开放阅读框编码一种与细菌D-丙氨酸：D-丙氨酸连接酶（形成ADP）（EC 6.3.2.4）具有显著相似性的蛋白质。预测的部分氨基酸序列与大肠杆菌ddl基因编码的蛋白质的氨基酸序列有33%的同源性。
