Catalytic Mechanism of the Hotdog-Fold Thioesterase PA1618 Revealed by X-ray Structure Determination of a Substrate-Bound Oxygen Ester Analogue Complex-Reference-Cited by-同舟云学术

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Catalytic Mechanism of the Hotdog-Fold Thioesterase PA1618 Revealed by X-ray Structure Determination of a Substrate-Bound Oxygen Ester Analogue Complex

Published:2017-08-30 Issue:19 Volume:18 Page:1935-1943
ISSN:1439-4227
Container-title:ChemBioChem
language:en
Short-container-title:ChemBioChem

Author:

Latham John A.¹^ORCID,Ji Tianyang²,Matthews Kaila³,Mariano Patrick S.³,Allen Karen N.²,Dunaway-Mariano Debra³

Affiliation:

1. Department of Chemistry and Biochemistry; University of Denver; Denver CO 80208-0183 USA

2. Department of Chemistry; Boston University; 590 Commonwealth Avenue Room 299 Boston MA 02215 USA

3. Department of Chemistry and Chemical Biology; University of New Mexico; Albuquerque NM 87131 USA

Funder

Foundation for the National Institutes of Health

Publisher

Wiley

Subject

Organic Chemistry,Molecular Biology,Molecular Medicine,Biochemistry

Reference32 articles.

1. The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism

2. Regulation of cellular signalling by fatty acid acylation and prenylation of signal transduction proteins

3. Fatty acyl-CoA thioesters are ligands of hepatic nuclear factor-4α

4. Enoyl-Coenzyme A Hydratase-Catalyzed Exchange of the .alpha.-Protons of Coenzyme A Thiol Esters: A Model for an Enolized Intermediate in the Enzyme-Catalyzed Elimination?

5. The Claisen condensation in biology

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