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Article

Structural basis for the activity and substrate specificity of fluoroacetyl-CoA thioesterase FlK.

The Journal of biological chemistry - 16 Jul 2010

Dias Marcio V B, Huang Fanglu, Chirgadze Dimitri Y, Tosin Manuela, Spiteller Dieter, Dry Emily F V, Leadlay Peter F, Spencer Jonathan B, Blundell Tom L

Abstract excerpt

The thioesterase FlK from the fluoroacetate-producing Streptomyces cattleya catalyzes the hydrolysis of fluoroacetyl-coenzyme A. This provides an effective self-defense mechanism, preventing any fluoroacetyl-coenzyme A formed from being further metabolized to 4-hydroxy-trans-aconitate, a lethal inhibitor of the tricarboxylic acid cycle. Remarkably, FlK does not accept acetyl-coenzyme A as a substrate. Crystal...

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Identifiers

PMID: 20430898
DOI: 10.1074/jbc.M110.107177
PMCID: PMC2903362

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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