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Literature summary extracted from

  • Hu, Z.; Spadafora, L.J.; Hajdin, C.E.; Bennett, B.; Crowder, M.W.
    Structure and mechanism of copper- and nickel-substituted analogues of metallo-beta -lactamase L1 (2009), Biochemistry, 48, 2981-2989.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
3.5.2.6 additional information lactamase CoCo-L1, enzyme containing transition metal ions other than Zn(2+), prepared and characterized by kinetic and spectroscopic studies Escherichia coli
3.5.2.6 additional information lactamase Cu-L1, Cu-containing analog of metallo-beta-lactamase L1. Enzyme containing transition metal ions other than Zn(2+), prepared and characterized by kinetic and spectroscopic studies Escherichia coli
3.5.2.6 additional information lactamase Ni-L1, Ni-containing analog of metallo-beta-lactamase L1. Enzyme containing transition metal ions other than Zn(2+), prepared and characterized by kinetic and spectroscopic studies Escherichia coli
3.5.2.6 additional information lactamase NiZn-L1, enzyme containing transition metal ions other than Zn(2+), prepared and characterized by kinetic and spectroscopic studies Escherichia coli
3.5.2.6 additional information lactamase ZnCo-L1, enzyme containing transition metal ions other than Zn(2+), prepared and characterized by kinetic and spectroscopic studies Escherichia coli
3.5.2.6 additional information lactamase ZnFe-L1, enzyme containing transition metal ions other than Zn(2+), prepared and characterized by kinetic and spectroscopic studies Escherichia coli
3.5.2.6 additional information lactamase ZnNi-L1, enzyme containing transition metal ions other than Zn(2+), prepared and characterized by kinetic and spectroscopic studies Escherichia coli
3.5.2.6 additional information lactamase ZnZn-L1, enzyme containing transition metal ions other than Zn(2+), prepared and characterized by kinetic and spectroscopic studies Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.2.6 0.002
-
 Imipenem lactamase ZnZn-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 0.008
-
 cefaclor lactamase ZnZn-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 0.013
-
 Imipenem lactamase CoCo-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 0.023
-
 Imipenem lactamase ZnCo-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 0.027
-
 Imipenem lactamase ZnFe-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 0.035
-
 cefaclor lactamase ZnFe-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 0.036
-
 penicillin G lactamase CoCo-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 0.04
-
 cefaclor lactamase ZnCo-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 0.042
-
 Imipenem lactamase Cu-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 0.043
-
 cefaclor lactamase CoCo-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 0.058
-
 cefaclor lactamase Cu-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 0.061
-
 Imipenem lactamase ZnNi-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 0.091
-
 cefaclor lactamase ZnNi-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 0.218
-
 penicillin G lactamase ZnCo-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 0.224
-
 nitrocefin lactamase Cu-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 0.278
-
 penicillin G lactamase ZnZn-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 16
-
 nitrocefin lactamase NiZn-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 18
-
 nitrocefin lactamase Ni-L1, 25°C, pH 7.0 Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.2.6 Cu2+ metalloenzyme Escherichia coli
3.5.2.6 additional information the metal binding sites, particularly the Zn2 site, in metallo-beta-lactamase L1 are very flexible and can accommodate a number of different divalent metal ions Escherichia coli
3.5.2.6 Ni2+ Ni2+ binds in the Zn2+-site and the ring-opened product coordinates Ni2+ Escherichia coli
3.5.2.6 Zn2+ metalloenzyme Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
3.5.2.6 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.2.6 cefaclor + H2O
-
 Escherichia coli (2R)-2-[(R)-{[(2R)-2-amino-2-phenylacetyl]amino}(carboxy)methyl]-5-chloro-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
 ?
3.5.2.6 imipenem + H2O
-
 Escherichia coli (5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
 ?
3.5.2.6 additional information the substituted lactamases Cu-L1 and ZnNi-L1 hydrolyze cephalosporins and carbapenems, but not penicillins, suggesting that the Zn2+-site modulates substrate preference in mbetal L1 Escherichia coli ?
-
 ?
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 penicillin G + H2O
-
 Escherichia coli (2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.2.6 mbetal L1
-
 Escherichia coli
3.5.2.6 metallo-beta-lactamase L1
-
 Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.2.6 3 6 nitrocefin lactamase NiZn-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 12
-
 Imipenem lactamase ZnCo-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 13
-
 Imipenem lactamase ZnZn-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 14
-
 cefaclor lactamase CoCo-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 16
-
 cefaclor lactamase ZnFe-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 24
-
 nitrocefin lactamase Ni-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 26
-
 cefaclor lactamase ZnCo-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 27
-
 cefaclor lactamase ZnNi-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 29
-
 cefaclor lactamase Cu-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 38
-
 cefaclor lactamase ZnZn-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 43
-
 Imipenem lactamase CoCo-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 59
-
 Imipenem lactamase ZnFe-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 96
-
 nitrocefin lactamase Cu-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 118
-
 penicillin G lactamase CoCo-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 166
-
 Imipenem lactamase ZnNi-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 205
-
 Imipenem lactamase Cu-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 692
-
 penicillin G lactamase ZnCo-L1, 25°C, pH 7.0 Escherichia coli
3.5.2.6 761
-
 penicillin G lactamase ZnZn-L1, 25°C, pH 7.0 Escherichia coli