Back to Search
Start Over
Increased Hydrolysis of Oximino-β-Lactams by CMY-107, a Tyr199Cys Mutant Form of CMY-2 Produced by Escherichia coli
- Source :
- Antimicrobial Agents and Chemotherapy. 59:7894-7898
- Publication Year :
- 2015
- Publisher :
- American Society for Microbiology, 2015.
-
Abstract
- The cephalosporinase CMY-107, a Tyr199Cys mutant form of CMY-2 encoded by an IncI self-transferable plasmid carried by an Escherichia coli clinical strain, was characterized. The enzyme hydrolyzed oximino-cephalosporins and aztreonam more efficiently than CMY-2 did.
- Subjects :
- Models, Molecular
Mutant
Gene Expression
chemical and pharmacologic phenomena
Microbial Sensitivity Tests
Aztreonam
medicine.disease_cause
complex mixtures
Protein Structure, Secondary
beta-Lactamases
Substrate Specificity
chemistry.chemical_compound
Hydrolysis
Plasmid
Mechanisms of Resistance
parasitic diseases
β lactams
Escherichia coli
medicine
Humans
Pharmacology (medical)
Cysteine
Escherichia coli Infections
Pharmacology
chemistry.chemical_classification
Strain (chemistry)
business.industry
Chemistry
Escherichia coli Proteins
bacterial infections and mycoses
Anti-Bacterial Agents
Cephalosporins
Protein Structure, Tertiary
Biotechnology
Isoenzymes
Kinetics
Infectious Diseases
Enzyme
Amino Acid Substitution
Biochemistry
Genetic Loci
Mutation
Tyrosine
business
therapeutics
Multilocus Sequence Typing
Plasmids
Subjects
Details
- ISSN :
- 10986596 and 00664804
- Volume :
- 59
- Database :
- OpenAIRE
- Journal :
- Antimicrobial Agents and Chemotherapy
- Accession number :
- edsair.doi.dedup.....fa8e212f9491f9c990b99c01442f5392
- Full Text :
- https://doi.org/10.1128/aac.01793-15