Publication | Open Access
Processing of Bacillus licheniformis penicillinases lacking a lipoprotein modification site in Escherichia coli
12
Citations
9
References
1986
Year
EngineeringBacteriologyMutant PrepenicillinaseMolecular BiologyEscherichia ColiChemical BiologyBacillus Licheniformis PenicillinasesEnzymatic ModificationBiosynthesisNew Penicillinase MutantsStructure-function Enzyme KineticsBiochemistryMolecular MicrobiologyClinical MicrobiologyProtein BiosynthesisLipoprotein Modification SiteCellular EnzymologyNatural SciencesPenp Ser-27 PrepenicillinaseBiotechnologySynthetic BiologyProtein EngineeringMicrobiologyMutagenesisMicrobial Genetics
We have previously shown that the penP Ser-27 prepenicillinase is processed into two forms, Ser-35-penicillinase and Asn-29 penicillinase. Two new penicillinase mutants, penP Ser-27 Pro-28 and penP Ser-27,23' (Pro-Asp)24', were derived from the penP Ser-27 mutant by oligonucleotide-directed site-specific mutagenesis. The penP Ser-27 Pro-28 mutant prepenicillinase was also processed into two forms, Ser-35-penicillinase and Gly-26-penicillinase. On the contrary, the penP Ser-27,23' (Pro-Asp)24' mutant prepenicillinase is unprocessed.
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