Martini F, Angelaccio S, Pascarella S, Barra D, Bossa F, Schirch V
J Biol Chem. 1987 Apr 25;262(12):5499-509.
The complete amino acid sequence of cytosolic serine hydroxymethyltransferase from rabbit liver was determined. The sequence was determined from analysis of peptides isolated from tryptic and cyanogen bromide cleavages of the enzyme. Special procedures were used to isolate and sequence the C-terminal and blocked N-terminal peptides. Each of the four identical subunits of the enzyme consists of 483 residues. The sequence could be easily aligned with the sequence of Escherichia coli serine hydroxymethyltransferase. The primary structural homology between the rabbit and E. coli enzymes is about 42%. The importance of the primary and predicted secondary structural homology between the two enzymes is discussed.
已确定兔肝胞质丝氨酸羟甲基转移酶的完整氨基酸序列。该序列是通过对从该酶的胰蛋白酶和溴化氰裂解产物中分离出的肽段进行分析而确定的。采用特殊方法分离并测序了C末端和被封闭的N末端肽段。该酶的四个相同亚基中的每一个都由483个残基组成。该序列能够很容易地与大肠杆菌丝氨酸羟甲基转移酶的序列比对。兔和大肠杆菌这两种酶之间的一级结构同源性约为42%。文中讨论了这两种酶之间一级结构和预测二级结构同源性的重要性。
