Reengineering the specificity of a serine active-site enzyme. Two active-site mutations convert a hydrolase to a transferase.

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Article

Reengineering the specificity of a serine active-site enzyme. Two active-site mutations convert a hydrolase to a transferase.

The Journal of biological chemistry - 7 Jan 1994

Witkowski A, Witkowska H E, Smith S

Abstract excerpt

Two residues are known to play important catalytic roles in fatty acyl-thioester hydrolase, thioesterase II: Ser-101, the site of a covalent acyl-enzyme intermediate, and His-237 which is within hydrogen bonding distance of Ser-101 and facilitates catalysis by increasing the nucleophilicity of th...

Topics

Acylation
Acyltransferases
Animals
Binding Sites
Biological Evolution
Fatty Acid Synthases
Kinetics
Mercaptoethanol
Mutation
Protein Engineering
Rats
Serine
Substrate Specificity
Sulfhydryl Compounds
Thiolester Hydrolases

Source

Open in PubMed

Identifiers

PMID: 8276823

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8276823-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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