Utilization of an active serine 101----cysteine mutant to demonstrate the proximity of the catalytic serine 101 and histidine 237 residues in thioesterase II.

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Article

Utilization of an active serine 101----cysteine mutant to demonstrate the proximity of the catalytic serine 101 and histidine 237 residues in thioesterase II.

The Journal of biological chemistry - 15 Sept 1992

Witkowski A, Naggert J, Witkowska H E, Randhawa Z I, Smith S

Abstract excerpt

Thioesterase II is a 29-kDa monomer which, in certain specialized tissues, acts as a chain terminator in fatty acid synthesis by hydrolyzing medium-chain fatty acids from the fatty acid synthase. As with serine proteases, hydrolysis appears to involve acylation of the active site serine residue (Ser-101) assisted by a histidine, tentatively identified as His-237. To determine whether in the folded protein His-237...

Topics

Amino Acid Sequence
Animals
Base Sequence
Binding Sites
Catalysis
Chromatography, High Pressure Liquid
Cross-Linking Reagents
Cysteine
DNA
Fatty Acid Synthases
Histidine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Kinetics

Mass Spectrometry

Molecular Sequence Data

Mutation

Propane

Rats

Serine

Source

Open in PubMed

Identifiers

PMID: 1526985

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1526985-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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