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Literature summary for 3.5.2.6 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

Protein Variants Comment Organism
additional information lactamase CoCo-L1, enzyme containing transition metal ions other than Zn(2+), prepared and characterized by kinetic and spectroscopic studies Escherichia coli
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
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
additional information lactamase NiZn-L1, enzyme containing transition metal ions other than Zn(2+), prepared and characterized by kinetic and spectroscopic studies Escherichia coli
additional information lactamase ZnCo-L1, enzyme containing transition metal ions other than Zn(2+), prepared and characterized by kinetic and spectroscopic studies Escherichia coli
additional information lactamase ZnFe-L1, enzyme containing transition metal ions other than Zn(2+), prepared and characterized by kinetic and spectroscopic studies Escherichia coli
additional information lactamase ZnNi-L1, enzyme containing transition metal ions other than Zn(2+), prepared and characterized by kinetic and spectroscopic studies Escherichia coli
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]

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

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ metalloenzyme Escherichia coli
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
Ni2+ Ni2+ binds in the Zn2+-site and the ring-opened product coordinates Ni2+ Escherichia coli
Zn2+ metalloenzyme Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
?
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
-
?
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 ?
-
?
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
-
?
penicillin G + H2O
-
Escherichia coli (2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
?

Synonyms

Synonyms Comment Organism
mbetal L1
-
Escherichia coli
metallo-beta-lactamase L1
-
Escherichia coli

Turnover Number [1/s]

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