p453-质粒介导的PIT-2β-内酰胺酶（SHV-1）的完整氨基酸序列
Complete amino acid sequence of p453-plasmid-mediated PIT-2 beta-lactamase (SHV-1).
作者信息
Barthélémy M, Peduzzi J, Labia R
机构信息
Muséum National d'Histoire Naturelle, C.N.R.S. U.A. 401, Paris, France.
出版信息
Biochem J. 1988 Apr 1;251(1):73-9. doi: 10.1042/bj2510073.
Abstract
The complete amino acid sequence of the p453-plasmid-mediated PIT-2 beta-lactamase (SHV-1) was determined. The protein contains 265 residues. Peptides resulting from digestions with trypsin, Staphylococcus aureus V8 proteinase, chymotrypsin and Lys-C proteinase and cleavage with CNBr were separated and purified by using reverse-phase h.p.l.c. The amino acid sequence of each peptide was manually determined with the dimethylaminoazobenzene isothiocyanate/phenyl isothiocyanate double-coupling method. The primary structure of PIT-2 beta-lactamase was compared with those of two closely related enzymes, namely TEM-1 beta-lactamase and the beta-lactamase of Klebsiella pneumoniae strain LEN-1. The PIT-2 beta-lactamase amino acid sequence was strongly retained, with respectively 68% and 88% homology. Thus PIT-2 enzyme could represent an evolutionary step between a chromosomally encoded beta-lactamase and the plasmid-mediated TEM beta-lactamases.
摘要
测定了p453质粒介导的PIT-2β-内酰胺酶（SHV-1）的完整氨基酸序列。该蛋白质含有265个残基。用胰蛋白酶、金黄色葡萄球菌V8蛋白酶、胰凝乳蛋白酶和Lys-C蛋白酶消化以及用溴化氰裂解产生的肽段，通过反相高效液相色谱法进行分离和纯化。使用二甲基氨基偶氮苯异硫氰酸酯/苯异硫氰酸酯双偶联法手动测定每个肽段的氨基酸序列。将PIT-2β-内酰胺酶的一级结构与另外两种密切相关的酶，即TEM-1β-内酰胺酶和肺炎克雷伯菌LEN-1菌株的β-内酰胺酶进行了比较。PIT-2β-内酰胺酶的氨基酸序列高度保守，同源性分别为68%和88%。因此，PIT-2酶可能代表了染色体编码的β-内酰胺酶和质粒介导的TEMβ-内酰胺酶之间的一个进化阶段。
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