Dihydrofolate reductase from amethopterin-resistant Lactobacillus casei.
Dihydrofolate reductase from amethopterin-resistant Lactobacillus casei.
复制标题
来自抗甲氨蝶呤干酪乳杆菌的二氢叶酸还原酶。
DOI：
10.1021/bi00756a011
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发表时间：
1972
期刊：
影响因子：
2.9
通讯作者：
F. M. Huennekens
中科院分区：
文献类型：
--
作者：
L. Gundersen;R. Dunlap;N. Harding;J. Freisheim;F. Otting;F. M. Huennekens
通过序列分析溴化氰、胰蛋白酶、葡萄球菌蛋白酶和粘蛋白酶切割产生的肽，确定了干酪乳杆菌耐氨甲喋呤菌株的二氢叶酸还原酶的完整氨基酸序列。将该序列与其他细菌来源的还原酶序列进行比较，表明这些酶是同源的。干酪乳杆菌还原酶序列显示出与大肠杆菌酶序列的29%序列同一性，与来自屎链球菌的酶序列的34%同一性。L. casei还原酶与S.屎室
The complete amino acid sequence of dihydrofolate reductase from an amethopterin-resistant strain of Lactobacillus casei has been determined by sequence analysis of peptides produced by cleavage with cyanogen bromide, trypsin, staphylococcal protease, and myxobatter protease. Comparison of this sequence with those of reductases from other bacterial sources shows that the enzymes are homologous. The Lactobacillus casei reductase sequence shows a 29% sequence identity with that of the Escherichia coli enzyme and a 34% identity with the sequence of the enzyme from Streptococcus faecium. The NHz-terminal 68 residues of the L. casei reductase show a 54% sequence identity with that of the enzyme from S. faecium.