铜绿假单胞菌前弹性蛋白酶原蛋白水解加工过程中涉及的切割位点的鉴定。

Identification of cleavage sites involved in proteolytic processing of Pseudomonas aeruginosa preproelastase.

作者信息

Kessler E, Safrin M, Peretz M, Burstein Y

机构信息

Maurice and Gabriela Goldschleger Eye Research Institute, Tel-Aviv University, Israel.

出版信息

FEBS Lett. 1992 Mar 16;299(3):291-3. doi: 10.1016/0014-5793(92)80134-3.

DOI:10.1016/0014-5793(92)80134-3

PMID:1544509

Abstract

The extracellular elastase (33 kDa) of Pseudomonas aeruginosa is synthesized as a 53.6 kDa preproenzyme containing a long, N-terminal propeptide. The free propeptide and the elastase precursor generated upon propeptide removal were isolated from P. aeruginosa cells and subjected to N-terminal amino acid sequence analysis. The results identified Ala-174 and Ala+1 as the amino terminal residues of the propeptide and the elastase precursor, respectively, indicating that: (1) the signal peptide consists of 23 amino acid residues and its molecular weight is 2.4 kDa, (2) the propeptide contains 174 amino acid residues and is of 18.1 kDa molecular weight, and (3) no additional N-terminal proteolytic cleavage is required for elastase maturation.

摘要

铜绿假单胞菌的细胞外弹性蛋白酶（33 kDa）最初以53.6 kDa的前体酶形式合成，该前体酶包含一个长的N端前肽。从前体肽去除后产生的游离前体肽和弹性蛋白酶前体从铜绿假单胞菌细胞中分离出来，并进行N端氨基酸序列分析。结果分别确定丙氨酸-174和丙氨酸+1为前体肽和弹性蛋白酶前体的氨基末端残基，这表明：（1）信号肽由23个氨基酸残基组成，分子量为2.4 kDa；（2）前体肽包含174个氨基酸残基，分子量为18.1 kDa；（3）弹性蛋白酶成熟不需要额外的N端蛋白水解切割。