A point mutation leads to altered product specificity in β-lactamase catalysis

Proceedings of the National Academy of Sciences of the United States of America

Volumn 94, Issue 2, 1997, Pages 443-447

  Lewis, Evan R ^a   Winterberg, Kelly M ^a   Fink, Anthony L ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

intramolecular rearrangement; mechanism; oxazolinone; penicillin

Indexed keywords

BETA LACTAMASE; OXAZOLINE DERIVATIVE; PENICILLIN DERIVATIVE;

ANTIBIOTIC RESISTANCE; ARTICLE; BACILLUS LICHENIFORMIS; DEACYLATION; ENZYME MECHANISM; ENZYME MODIFICATION; ENZYME SPECIFICITY; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL;

ASPARAGINE; BACILLUS; BETA-LACTAMASES; CARBOXYPEPTIDASES; CATALYSIS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; LEUCINE; MAGNETIC RESONANCE SPECTROSCOPY; MASS SPECTROMETRY; PENICILLIN G; POINT MUTATION; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

BACILLUS LICHENIFORMIS;

EID: 0031037145     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.94.2.443     Document Type: Article

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