Katzenmeier G, Schmid C, Kellermann J, Lottspeich F, Bacher A
Lehrstuhl für Organische Chemie und Biochemie, Technische Universität München.
Biol Chem Hoppe Seyler. 1991 Nov;372(11):991-7. doi: 10.1515/bchm3.1991.372.2.991.
The sequence of the gene coding for GTP cyclohydrolase I of Escherichia coli and of the adjacent regions was determined. The open reading frame contains 669 nucleotides. The deduced amino-acid sequence represents a protein consisting of 223 amino-acid residues with a molecular mass of 24,873 Da. Partial amino-acid sequences of the N-terminal region and of 5 peptides obtained by trypsin and BrCN cleavage were determined by Edman degradation and were in full agreement with the sequence deduced from the nucleotide sequence. The starting methionine is removed by posttranslational modification. The protein shows extensive homology to the recently reported GTP cyclohydrolase from rats.
测定了大肠杆菌GTP环化水解酶I编码基因及其相邻区域的序列。开放阅读框包含669个核苷酸。推导的氨基酸序列代表一种由223个氨基酸残基组成的蛋白质，分子量为24,873道尔顿。通过埃德曼降解法测定了N端区域以及经胰蛋白酶和溴化氰裂解得到的5个肽段的部分氨基酸序列，这些序列与从核苷酸序列推导的序列完全一致。起始甲硫氨酸通过翻译后修饰被去除。该蛋白质与最近报道的大鼠GTP环化水解酶具有广泛的同源性。
