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Article

The intrachain disulfide bridge is responsible of the unusual stability properties of novel acylphosphatase from Escherichia coli.

FEBS letters - 22 Dec 2006

Ramazzotti Matteo, Parrini Claudia, Stefani Massimo, Manao Giampaolo, Degl'Innocenti Donatella

Abstract excerpt

Acylphosphatase (AcP) activity in prokaryotes was classically attributed to some aspecific acid phosphatases. We identified an open reading frame for a putative AcP in the b0968 Escherichia coli gene and purified the recombinant enzyme after checking by RT-PCR that it was indeed expressed. EcoAcP has a predicted typical fold of the AcP family but displays a very low specific activity and a high structural...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 17134700
DOI: 10.1016/j.febslet.2006.11.033

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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