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Article

Saturation mutagenesis of Asn152 reveals a substrate selectivity switch in P99 cephalosporinase.

Protein science : a publication of the Protein Society - 1 Dec 2007

Lefurgy Scott T, de Jong René M, Cornish Virginia W

Abstract excerpt

In class C beta-lactamases, the strictly conserved Asn152 forms part of an extended active-site hydrogen-bonding network. To probe its role in catalysis, all 19 mutants of Enterobacter cloacae P99 cephalosporinase Asn152 were simultaneously constructed and screened in Escherichia coli for their in vivo activity. The screen identified the previously uncharacterized mutants Asn152Ser, Asn152Thr, and Asn152Gly,...

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Identifiers

PMID: 18029418
DOI: 10.1110/ps.073092407
PMCID: PMC2222824

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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