Zhuang Zhihao, Song Feng, Martin Brian M, Dunaway-Mariano Debra
Department of Chemistry, University of New Mexico, Albuquerque, NM 87131, USA.
FEBS Lett. 2002 Apr 10;516(1-3):161-3. doi: 10.1016/s0014-5793(02)02533-4.
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.
