Partial amino acid sequence of penicillinase coded by Escherichia coli plasmid R6K.
- 1 August 1978
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 75 (8) , 3732-3736
- https://doi.org/10.1073/pnas.75.8.3732
Abstract
Direct studies of the amino acid sequence of an E. coli plasmid-coded penicillinase (penicillin amido-.beta.-lactamhydrolase, EC 3.5.2.6) are in complete agreement with results derived from the translation of the DNA sequence of a related plasmid, apart from a single amino acid substitution. This penicillinase from a gram-negative bacterium shows 30-35% identity with functionally similar enzymes from gram-positve bacteria.This publication has 16 references indexed in Scilit:
- Nucleotide sequence of the ampicillin resistance gene of Escherichia coli plasmid pBR322.Proceedings of the National Academy of Sciences, 1978
- A new method for sequencing DNA.Proceedings of the National Academy of Sciences, 1977
- 5.5 Å crystallographic structure of penicillin β-lactamase and radius of gyration in solutionJournal of Molecular Biology, 1976
- The partial amino acid sequence of the extracellular β-lactamase I of Bacillus cereus 569/HBiochemical Journal, 1975
- The amino acid sequence of cytochromes c-551 from three species of PseudomonasBiochemical Journal, 1973
- The β-Lactamases of Gram-Negative Bacteria and their Possible Physiological RolePublished by Elsevier ,1973
- Preparation of gram quantities of a purified R-factor-mediated penicillinase from Escherichia coli strain W3310Biochemical Journal, 1972
- Application of sequenator analysis to the study of proteinsBiochemistry, 1972
- Chemical Structure of Bacterial PenicillinasesNature, 1969
- Penicillinase Synthesis Controlled By Infectious R Factors In EnterobacteriaceaeNature, 1965