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Dalton Transactions, ISSN 1477-9226, 12/2013, Volume 43, Issue 3, pp. 91 - 928
Journal Article
Journal Article
Biochemical Journal, ISSN 0264-6021, 12/2010, Volume 432, Issue 3, pp. 565 - 573
The OP (organophosphate)-degrading enzyme from Agrobacterium radiobacter (OpdA) is a binuclear metallohydrolase able to degrade highly toxic OP pesticides and... 
Site-directed mutagenesis | Agrobacterium radiobacter | Organophosphate pesticide | Organophosphate-degrading enzyme | OpdA | Hydrogen bonding | Crystal structure | site-directed mutagenesis | organophosphate-degrading enzyme | COMPLEX | PHOSPHOTRIESTERASE | ACTIVE-SITE | BIOCHEMISTRY & MOLECULAR BIOLOGY | HYDROLYSIS | MODEL | 3-DIMENSIONAL STRUCTURE | hydrogen bonding | BINUCLEAR METAL CENTER | SUBSTRATE | BIOREMEDIATOR GLYCEROPHOSPHODIESTERASE | crystal structure | organophosphate pesticide | BINDING | Phosphoric Triester Hydrolases - isolation & purification | Bacterial Proteins - chemistry | Substrate Specificity | Crystallography, X-Ray | Mutant Proteins - isolation & purification | Rhizobium - enzymology | Organophosphorus Compounds - metabolism | Recombinant Proteins - isolation & purification | Metalloproteins - metabolism | Metalloproteins - genetics | Phosphoric Triester Hydrolases - chemistry | Metals, Heavy - chemistry | Pesticides - metabolism | Tyrosine - chemistry | Recombinant Proteins - metabolism | Catalytic Domain | Biocatalysis | Mutagenesis, Site-Directed | Phosphoric Triester Hydrolases - genetics | Bacterial Proteins - genetics | Recombinant Proteins - chemistry | Mutant Proteins - metabolism | Arginine - chemistry | Rhizobium - genetics | Rhizobium - metabolism | Metalloproteins - chemistry | Cations, Divalent | Hydrogen Bonding | Mutant Proteins - chemistry | Bacterial Proteins - metabolism | Phosphoric Triester Hydrolases - metabolism | Protein Conformation | Kinetics | Bacterial Proteins - isolation & purification | Hydrogen-Ion Concentration
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 6/2013, Volume 110, Issue 25, pp. 10177 - 10182
Journal Article
Scientific Reports, ISSN 2045-2322, 01/2017, Volume 7, Issue 1, pp. 40357 - 40357
Metallo-beta-lactamases (MBLs) with activity towards a broad-spectrum of beta-lactam antibiotics have become a major threat to public health, not least due to... 
REFINEMENT | SUBSTRATE-SPECIFICITY | METALLO-BETA-LACTAMASE | PSEUDOMONAS-AERUGINOSA | TERMINAL HALF | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | CRYSTAL-STRUCTURES | MUTATIONS | METALLOHYDROLASES | RNASE E | Enzymes | Antibiotics | Mutagenesis | β-Lactam antibiotics | Antibiotic resistance | Evolution | Mutation | Saturation mutagenesis | Public health | Crystal structure | Index Medicus
Journal Article