Distinct physiological roles for the two L-asparaginase isozymes of Escherichia coli

被引：32

作者：

Srikhanta, Yogitha N. ^{[2
]}

Atack, John M. ^{[1
]}

Beacham, Ifor R. ^{[1
]}

Jennings, Michael P. ^{[1
]}

机构：

[1] Griffith Univ, Inst Glyc, Gold Coast, Qld 4222, Australia

[2] Univ Melbourne, Dept Microbiol & Immunol, Melbourne, Vic 3010, Australia

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2013年 / 436卷 / 03期

基金：

澳大利亚国家健康与医学研究理事会;

关键词：

Escherichia coli; Asparaginase; Anaerobic growth; Isozymes; GENE-EXPRESSION; ANSA GENE; FNR; PROTEIN; NITRATE; K-12; CRP;

D O I：

10.1016/j.bbrc.2013.05.066

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Escherichia coli expresses two L-asparaginase (EC 3.5.1.1) isozymes: L-asparaginse I, which is a low affinity, cytoplasmic enzyme that is expressed constitutively, and L-asparaginase II, a high affinity periplasmic enzyme that is under complex co-transcriptional regulation by both Fnr and Crp. The distinct localisation and regulation of these enzymes suggest different roles. To define these roles, a set of isogenic mutants was constructed that lacked either or both enzymes. Evidence is provided that L-asparaginase II, in contrast to L-asparaginase I, can be used in the provision of an anaerobic electron acceptor when using a non-fermentable carbon source in the presence of excess nitrogen. (C) 2013 Published by Elsevier Inc.

引用

页码：362 / 365

页数：4

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