期刊论文详细信息
FEBS Letters
The YbgC protein encoded by the ybgC gene of the tol‐pal gene cluster of Haemophilus influenzae catalyzes acyl‐coenzyme A thioester hydrolysis
Dunaway-Mariano, Debra1  Martin, Brian M2  Song, Feng1  Zhuang, Zhihao1 
[1] Department of Chemistry, University of New Mexico, Albuquerque, NM 87131, USA;Clinical Neuroscience Branch of the National Institute of Mental Health, Bldg. 49 B1EE16, 49 Convent Dr., Bethesda, MD 20892–4404, USA
关键词: Tol-pal operon;    Thioesterase;    Haemophilus influenzae;    YbgC;    Bacterial cell envelope;    Peptidoglycan;   
DOI  :  10.1016/S0014-5793(02)02533-4
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

This paper examines the catalytic function of the protein YbgC, encoded by the ybgC gene of the tol-pal gene cluster in Haemophilus influenzae. The YbgC protein, a homologue of the Pseudomonas sp. strain CBS3 4-hydroxybenzoyl-coenzyme A thioesterase, conserves the active site Asp residue associated with thioesterase activity. The H. influenzae ybgC gene was cloned and overexpressed in Escherichia coli. The recombinant protein was purified and tested for thioesterase activity towards acyl-CoA and acyl-N-acetylcysteamine thioesters. The YbgC protein catalyzes the hydrolysis of short chain aliphatic acyl-CoA thioesters, while the D18N YbgC mutant protein (prepared to serve as a control) does not.

【 授权许可】

Unknown   

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