Literature DB >> 11959124

The YbgC protein encoded by the ybgC gene of the tol-pal gene cluster of Haemophilus influenzae catalyzes acyl-coenzyme A thioester hydrolysis.

Zhihao Zhuang1, Feng Song, Brian M Martin, Debra Dunaway-Mariano.   

Abstract

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.

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Year:  2002        PMID: 11959124     DOI: 10.1016/s0014-5793(02)02533-4

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  18 in total

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Authors:  María A Llamas; Juan L Ramos; José J Rodríguez-Herva
Journal:  J Bacteriol       Date:  2003-01       Impact factor: 3.490

Review 2.  Thioesterases: a new perspective based on their primary and tertiary structures.

Authors:  David C Cantu; Yingfei Chen; Peter J Reilly
Journal:  Protein Sci       Date:  2010-07       Impact factor: 6.725

3.  The hotdog thioesterase EntH (YbdB) plays a role in vivo in optimal enterobactin biosynthesis by interacting with the ArCP domain of EntB.

Authors:  Damien Leduc; Aurélia Battesti; Emmanuelle Bouveret
Journal:  J Bacteriol       Date:  2007-08-03       Impact factor: 3.490

4.  Mutation in a "tesB-like" hydroxyacyl-coenzyme A-specific thioesterase gene causes hyperproduction of extracellular polyhydroxyalkanoates by Alcanivorax borkumensis SK2.

Authors:  Julia S Sabirova; Manuel Ferrer; Heinrich Lünsdorf; Victor Wray; Rainer Kalscheuer; Alexander Steinbüchel; Kenneth N Timmis; Peter N Golyshin
Journal:  J Bacteriol       Date:  2006-09-22       Impact factor: 3.490

5.  Defective O-antigen polymerization in tolA and pal mutants of Escherichia coli in response to extracytoplasmic stress.

Authors:  Enrique D Vinés; Cristina L Marolda; Aran Balachandran; Miguel A Valvano
Journal:  J Bacteriol       Date:  2005-05       Impact factor: 3.490

6.  Thioesterase enzyme families: Functions, structures, and mechanisms.

Authors:  Benjamin T Caswell; Caio C de Carvalho; Hung Nguyen; Monikrishna Roy; Tin Nguyen; David C Cantu
Journal:  Protein Sci       Date:  2022-01-04       Impact factor: 6.725

Review 7.  Active site comparisons and catalytic mechanisms of the hot dog superfamily.

Authors:  Jason W Labonte; Craig A Townsend
Journal:  Chem Rev       Date:  2012-12-03       Impact factor: 60.622

8.  Identification of a hotdog fold thioesterase involved in the biosynthesis of menaquinone in Escherichia coli.

Authors:  Minjiao Chen; Xinyu Ma; Xiaolei Chen; Ming Jiang; Haigang Song; Zhihong Guo
Journal:  J Bacteriol       Date:  2013-04-05       Impact factor: 3.490

9.  Structure and function of a Campylobacter jejuni thioesterase Cj0915, a hexameric hot dog fold enzyme.

Authors:  Takeshi Yokoyama; Kyoung-Jae Choi; Anne M Bosch; Hye-Jeong Yeo
Journal:  Biochim Biophys Acta       Date:  2009-03-17

10.  Analysis of proteins with the 'hot dog' fold: prediction of function and identification of catalytic residues of hypothetical proteins.

Authors:  Lakshmi S Pidugu; Koustav Maity; Karthikeyan Ramaswamy; Namita Surolia; Kaza Suguna
Journal:  BMC Struct Biol       Date:  2009-05-28
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