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Literature summary extracted from

  • Che, T.; Bethel, C.R.; Pusztai-Carey, M.; Bonomo, R.A.; Carey, P.R.
    The different inhibition mechanisms of OXA-1 and OXA-24 beta-lactamases are determined by the stability of active site carboxylated lysine (2014), J. Biol. Chem., 289, 6152-6164.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.2.6 gene blaOXA-1, recombinant expression in Escerichia coli strain BL21(DE3) Escherichia coli
3.5.2.6 gene OXA24, recombinant expression in Escerichia coli strain BL21(DE3) Acinetobacter baumannii

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.2.6 purified recombinant enzyme, hanging drop vapor diffusion method, mixing of 6 mg/ml protein in 10 mM HEPES, pH 7.5, with crystallization solution containing 0.1 M HEPES, pH 7.5, 0.1 M sodium acetate, and 28% PEG 2000, X-ray diffraction structure determination and analysis Acinetobacter baumannii
3.5.2.6 purified recombinant enzyme, hanging drop vapor diffusion method, mixing of 9 mg/ml protein solution with crystallization solution containing 0.05 M HEPES, pH 7.5, and 15% PEG 8000, X-ray diffraction structure determination and analysis Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.2.6 BRL 42715
-
 Acinetobacter baumannii
3.5.2.6 BRL 42715
-
 Escherichia coli
3.5.2.6 nitrocefin substrate inhibition, NaHCO3 can reactivate the enzyme Acinetobacter baumannii
3.5.2.6 penem 1 a 6-methylidene penem, the carboxylated Lys84 in the active site of OXA-24 utilizes a catalytic water molecule to deacylate the Ser81, resulting in hydrolysis of the penem 1 inhibitor, and the enzyme is regenerated because Lys84 is not decarboxylated and hydrolyzes the next arriving inhibitor molecule, proposed mechanism for penem 1 and OXA-24, overview Acinetobacter baumannii
3.5.2.6 penem 1 a 6-methylidene penem, proposed mechanism for penem 1 and OXA-1, overview. Penem 1 can also cause the essentially irreversible decarboxylation of OXA-1 Escherichia coli
3.5.2.6 penem 3 a 6-methylidene penem Acinetobacter baumannii
3.5.2.6 penem 3 a 6-methylidene penem Escherichia coli
3.5.2.6 SA-1-204 a penam sulfone inhibitor, can effectively inhibit OXA-24 by decarboxylating the Lys84 in the active site Acinetobacter baumannii
3.5.2.6 SA-1-204 a penam sulfone inhibitor Escherichia coli
3.5.2.6 tazobactam
-
 Acinetobacter baumannii
3.5.2.6 tazobactam
-
 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.2.6 additional information
-
 additional information steady-state kinetics Escherichia coli
3.5.2.6 additional information
-
 additional information steady-state kinetics Acinetobacter baumannii
3.5.2.6 0.0083
-
 nitrocefin pH 7.2, temperature not specified in the publication, recombinant enzyme Escherichia coli
3.5.2.6 0.028
-
 nitrocefin pH 7.2, temperature not specified in the publication, recombinant enzyme Acinetobacter baumannii

Organism

EC Number Organism UniProt Comment Textmining
3.5.2.6 Acinetobacter baumannii J9XTR7 gene OXA24
-
3.5.2.6 Escherichia coli P13661 gene blaOXA-1
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.5.2.6 a beta-lactam + H2O = a substituted beta-amino acid overall mechanism for beta-lactamase-inhibitor reaction, Quantum mechanical/molecular mechanical calculations and Raman spectral analysis, overview Acinetobacter baumannii
a
3.5.2.6 a beta-lactam + H2O = a substituted beta-amino acid overall mechanism for beta-lactamase-inhibitor reaction, Quantum mechanical/molecular mechanical calculations and Raman spectral analysis, overview. The protonation of the zeta-nitrogen leads to a barrierless decarboxylation of the lysine carbamate Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.2.6 (5R,6E)-6-[(4H,6H-pyrazolo[1,5-c][1,3]thiazol-2-yl)methylidene]-4-thia-1-azabicyclo[3.2.0]hept-2-en-7-one + H2O
-
 Acinetobacter baumannii (2E)-2-[(2R)-2,3-dihydro-1,3-thiazol-2-yl]-3-(4H,6H-pyrazolo[1,5-c][1,3]thiazol-2-yl)prop-2-enoic acid
-
 ?
3.5.2.6 (5R,6Z)-6-[(1,6,7,8a-tetrahydro-5H-imidazo[2,1-b][1,3]oxazin-2-yl)methylidene]-4-thia-1-azabicyclo[3.2.0]hept-2-en-7-one + H2O
-
 Acinetobacter baumannii (2Z)-2-[(2R)-2,3-dihydro-1,3-thiazol-2-yl]-3-(1,6,7,8a-tetrahydro-5H-imidazo[2,1-b][1,3]oxazin-2-yl)prop-2-enoic acid
-
 ?
3.5.2.6 nitrocefin + H2O
-
 Escherichia coli (2R)-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
 ?
3.5.2.6 nitrocefin + H2O
-
 Acinetobacter baumannii (2R)-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.2.6 carbapenemase UniProt Acinetobacter baumannii
3.5.2.6 class D beta-lactamase
-
 Escherichia coli
3.5.2.6 class D beta-lactamase
-
 Acinetobacter baumannii
3.5.2.6 OXA-1
-
 Escherichia coli
3.5.2.6 oxa-1 beta-lactamase
-
 Escherichia coli
3.5.2.6 OXA-24
-
 Acinetobacter baumannii
3.5.2.6 OXA-24 beta-lactamase
-
 Acinetobacter baumannii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.2.6 7.2
-
 assay at Escherichia coli
3.5.2.6 7.2
-
 assay at Acinetobacter baumannii

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.5.2.6 additional information
-
 additional information inhibition kinetics Escherichia coli
3.5.2.6 additional information
-
 additional information inhibition kinetics Acinetobacter baumannii
3.5.2.6 0.00003
-
 penem 1 pH 7.2, temperature not specified in the publication, recombinant enzyme Acinetobacter baumannii
3.5.2.6 0.00005
-
 penem 1 pH 7.2, temperature not specified in the publication, recombinant enzyme Escherichia coli
3.5.2.6 0.00015
-
 penem 3 pH 7.2, temperature not specified in the publication, recombinant enzyme Acinetobacter baumannii
3.5.2.6 0.00038
-
 penem 3 pH 7.2, temperature not specified in the publication, recombinant enzyme Escherichia coli

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
3.5.2.6 0.00003
-
 pH 7.2, temperature not specified in the publication, recombinant enzyme Escherichia coli penem 1
3.5.2.6 0.00006
-
 pH 7.2, temperature not specified in the publication, recombinant enzyme Escherichia coli penem 3
3.5.2.6 0.00015
-
 pH 7.2, temperature not specified in the publication, recombinant enzyme Acinetobacter baumannii penem 1
3.5.2.6 0.00016
-
 pH 7.2, temperature not specified in the publication, recombinant enzyme Acinetobacter baumannii penem 3