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Article

Mutations of penicillin acylase residue B71 extend substrate specificity by decreasing steric constraints for substrate binding.

The Biochemical journal - 1 Apr 2003

Morillas Manuel, McVey Colin E, Brannigan James A, Ladurner Andreas G, Forney Larry J, Virden Richard

Abstract excerpt

Two mutant forms of penicillin acylase from Escherichia coli strains, selected using directed evolution for the ability to use glutaryl-L-leucine for growth [Forney, Wong and Ferber (1989) Appl. Environ. Microbiol. 55, 2550-2555], are changed within one codon, replacing the B-chain residue Phe(B71) with either Cys or Leu. Increases of up to a factor of ten in k (cat)/ K (m) values for substrates possessing a...

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Identifiers

PMID: 12511194
DOI: 10.1042/BJ20021383
PMCID: PMC1223260

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Source receipt: pubmed, retrieved 7 Sept 2026.

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