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Literature summary for 3.5.2.6 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.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression in Escherichia coli strain BL21(DE3) Salmonella enterica

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Inhibitors Comment Organism Structure
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
tazobactam strong inhibition by the mechanism-based inhibitor Salmonella enterica

Organism

Organism UniProt Comment Textmining
Salmonella enterica
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serovar Typhimurium, transferable plasmid blaPER-2 in a ceftibuten-resistant strain
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ceftazidime + H2O
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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
-
?
additional information oxyimino-cephalosporin substrates, interaction and binding structure, modeling, overview Salmonella enterica ?
-
?

Synonyms

Synonyms Comment Organism
PER-2
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Salmonella enterica

General Information

General Information Comment Organism
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
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