title: Processing of Bacillus licheniformis penicillinases lacking a lipoprotein modification site in Escherichia coli.
abstract: 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.
mesh_terms: D001407:Bacillus / Q000201:enzymology* / Q000235:genetics; D002462:Cell Membrane / Q000201:enzymology; D003593:Cytoplasm / Q000201:enzymology; D010450:Endopeptidases / Q000378:metabolism; D004792:Enzyme Precursors / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology / Q000378:metabolism*; D007700:Kinetics; D008074:Lipoproteins / Q000378:metabolism; D008565:Membrane Proteins; D009154:Mutation; D010405:Penicillinase / Q000235:genetics / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D012697:Serine Endopeptidases
chemical_list: D004792:Enzyme Precursors; D008074:Lipoproteins; D008565:Membrane Proteins; D010450:Endopeptidases; D012697:Serine Endopeptidases; C026515:type I signal peptidase; D010405:Penicillinase; C034279:prepenicillinase