Literature summary extracted from
Ruggiero, M.; Kerff, F.; Herman, R.; Sapunaric, F.; Galleni, M.; Gutkind, G.; Charlier, P.; Sauvage, E.; Power, P.
Crystal structure of the extended-spectrum beta-lactamase PER-2 and insights into the role of specific residues in the interaction with beta-lactams and beta-lactamase inhibitors (2014), Antimicrob. Agents Chemother., 58, 5994-6002.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
3.5.2.6 |
recombinant expression in Escherichia coli strain BL21(DE3) |
Salmonella enterica |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
3.5.2.6 |
purified recombinant enzyme, hanging drop vapor diffusion method, mixing of 0.0025 ml of 3.5mg/ml protein in , with 0.001 ml of crystallization solution containing 0.1 M HEPES in 1.5 M sodium citrate, pH 7.5, equilibration against 1.0 ml crystallization solution, 20°C, X-ray diffraction structure determination and analyysis at 2.2 A resolution, modeling |
Salmonella enterica |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
3.5.2.6 |
clavulanate |
strong inhibition by the mechanism-based inhibitor, Gln69, Arg220, Thr237, and probably Arg240A might be important in the stabilization of the clavulanate molecule, simulations, overview |
Salmonella enterica |
|
3.5.2.6 |
tazobactam |
strong inhibition by the mechanism-based inhibitor |
Salmonella enterica |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.5.2.6 |
Salmonella enterica |
- |
serovar Typhimurium, transferable plasmid blaPER-2 in a ceftibuten-resistant strain |
- |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
3.5.2.6 |
ceftazidime + H2O |
- |
Salmonella enterica |
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino](carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate |
- |
? |
|
3.5.2.6 |
additional information |
oxyimino-cephalosporin substrates, interaction and binding structure, modeling, overview |
Salmonella enterica |
? |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
3.5.2.6 |
PER-2 |
- |
Salmonella enterica |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
3.5.2.6 |
evolution |
PER-2 belongs to a small group of extended-spectrum beta-lactamases. Enzyme PER-2 is defined by the presence of a singular trans bond between residues 166 to 167, which generates an inverted omega loop, an expanded fold of this domain that results in a wide active site cavity that allows for efficient hydrolysis of antibiotics like the oxyimino-cephalosporins, and a series of exclusive interactions between residues not frequently involved in the stabilization of the active site in other class A beta-lactamases. PER beta-lactamases might be included within a cluster of evolutionarily related enzymes harboring the conserved residues Asp136 and Asn179 |
Salmonella enterica |
3.5.2.6 |
additional information |
secondary structures and conserved motifs of PER-2 and other class A beta-lactamases, presence of a hydrogen-bond network connecting Ser70-Gln69-water-Thr237-Arg220 that might be important for the proper activity and inhibition of the enzyme, strcture comparisson, simulation and modeling, overview |
Salmonella enterica |