Biochemical Journal · 1984 · 50 citations · 16 references
Life SciencesBiochemistryMicrobiologyBacteriologyEnzyme MechanismEnzymologyActive Site ArchitectureEnzyme Active SitesEnzyme InhibitionEnzyme KineticsEnzyme-substrate RecognitionActive Site AnalysisActive Site Residue ConservationActive Site Residue IdentificationActive Site StructureAmpc Beta-lactamasesBeta-lactamase GenesBeta-lactamase Structure-function RelationshipsSerine Beta-lactamases
Labelling the beta-lactamase of Enterobacter cloacae P99 with a poor substrate or a mechanism-based inactivator points to an active-site serine residue in a sequence closely resembling that of the ampC beta-lactamase. These results establish the P99 enzyme as a class-C beta-lactamase, and the concurrence of the two approaches helps to confirm the reliability of determining active-site sequences with the aid of mechanism-based inactivators.
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A gas-liquid solid phase peptide and protein sequenator.
Rodney M. Hewick, Michael W. Hunkapiller, Leroy Hood et al. · Journal of Biological Chemistry · 1981 · 2.2K citations · Full text
B Jaurin, Thomas Grundström · Proceedings of the National Academy of Sciences · 1981 · 386 citations · Full text