Identification of a type III thioesterase reveals the function of an operon crucial for Mtb virulence.

Identification of a type III thioesterase reveals the function of an operon crucial for Mtb virulence. Research Abstract Details 

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Identification of a type III thioesterase reveals the function of an operon crucial for Mtb virulence. Abstract Text:

Feng Wang,Robert Langley,Gulcin Gulten,Lei Wang,James C Sacchettini,

Rv0098 is part of an operon, Rv0096-Rv0101, from Mycobacterium tuberculosis (Mtb) that is essential for Mtb's survival in mouse macrophages. This operon also contains an acyl carrier protein and one of the only two nonribosomal peptide synthases in Mtb. Rv0098 is annotated in the genome as a hypothetical protein and was proposed to be an acyl-coenzyme A (CoA) dehydratase. The structure of Rv0098, together with subsequent biochemical analysis, indicated that Rv0098 is a long-chain fatty acyl-CoA thioesterase (FcoT). However, FcoT lacks a general base or a nucleophile that is always found in the catalytic site of type II and type I thioesterases, respectively. The active site of Mtb FcoT reveals the structural basis for its substrate specificity for long-chain acyl-CoA and allows us to propose a catalytic mechanism for the enzyme. The characterization of Mtb FcoT provides a putative function of this operon that is crucial for Mtb pathogenicity.

Identification of a type III thioesterase reveals the function of an operon crucial for Mtb virulence. Publishing Authors By Initials

F Wang,R Langley,G Gulten,L Wang,JC Sacchettini,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research

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Identification of a type III thioesterase reveals the function of an operon crucial for Mtb virulence. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Chemistry & biology

VOLUME: 14

Page Numbers: 543-51

Journal Abbreviation: Chem. Biol.

ISSN: 1074-5521

DAY: 3

MONTH: May

YEAR: 2007

Identification of a type III thioesterase reveals the function of an operon crucial for Mtb virulence. Information

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LANGUAGE: eng

NlmUniqueID: 9500160

Identification of a type III thioesterase reveals the function of an operon crucial for Mtb virulence. Keywords Mesh Terms:

KEYWORDS: Substrate Specificity

MESH TERMS: physiology

Chemical & Substance for Abstract: Identification of a type III thioesterase reveals the function of an operon crucial for Mtb virulence. Information

Substance Name: Palmitoyl-CoA Hydrolase

Registry Number: EC 3.1.2.2

Grant and Affiliation Information for Identification of a type III thioesterase reveals the function of an operon crucial for Mtb virulence.

AFFILIATION: Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA.

Country: England

AGENCY: United States NIAID

GRANT: P01AI068135

ACRONYM: AI

MEDLINETA: Chem Biol

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