Cloning and characterization of EstC from Burkholderia gladioli, a novel-type esterase related to plant enzymes

被引：23

作者：

Reiter, B ^{[1
]}

Glieder, A ^{[1
]}

Talker, D ^{[1
]}

Schwab, H ^{[1
]}

机构：

[1] Graz Univ Technol, Inst Biotechnol, A-8010 Graz, Austria

来源：

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY | 2000年 / 54卷 / 06期

基金：

奥地利科学基金会;

关键词：

D O I：

10.1007/s002530000468

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

By screening a genomic library of Brukholderia gladioli (formerly Pseudomonas marginata) for clones exhibiting esterolytic activity, the gene for a novel-type esterase (EstC) showing significant homology to plant enzymes could be isolated. High homology was found to two hydroxynitrile lyases originating from Hevea brasiliensis (tropical rubber tree) and Manihot esculenta (cassava), and to two proteins from Oryza sativa (rice) that are specifically induced upon infection by Pseudomonas syringae pv. syringae. The sequenced ORF encodes for a protein of 298 amino acids. The enzyme was efficiently overexpressed in Escherichia coli, purified and characterized with respect to enzymatic capabilities. The enzyme was able to hydrolyze a variety of esterase substrates of low to medium carbonic acid chain length, but no triglycerides were hydrolyzed. Despite the high sequence homology, no hydroxynitrile lyase activity could be recognized.

引用

页码：778 / 785

页数：8

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