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Article

A Single-Site Mutation at Ser146 Expands the Reactivity of the Oxygenase Component of p-Hydroxyphenylacetate 3-Hydroxylase.

ACS chemical biology - 21 Oct 2016

Dhammaraj Taweesak, Pinthong Chatchadaporn, Visitsatthawong Surawit, Tongsook Chanakan, Surawatanawong Panida, Chaiyen Pimchai

Abstract excerpt

The oxygenase component (C2) of p-hydroxyphenylacetate (4-HPA) 3-hydroxylase (HPAH) from Acinetobacter baumannii catalyzes the hydroxylation of various phenolic acids. In this report, we found that substitution of a residue close to the phenolic group binding site to yield the S146A variant resulted in an enzyme that is more effective than the wild-type in catalyzing the hydroxylation of 4-aminophenylacetate...

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Identifiers

PMID: 27541707
DOI: 10.1021/acschembio.6b00402

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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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