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Literature summary for 3.5.2.6 extracted from

  • Oguri, T.; Furuyama, T.; Okuno, T.; Ishii, Y.; Tateda, K.; Bonomo, R.A.; Shimizu-Ibuka, A.
    Crystal structure of Mox-1, a unique plasmid-mediated class C beta-lactamase with hydrolytic activity towards moxalactam (2014), Antimicrob. Agents Chemother., 58, 3914-3920.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
Mox-1 is a unique plasmid-mediated class C beta-lactamase, recombinant expression of His-tagged enzyme in Escherichia coli BL21(DE3)/pLysS Klebsiella pneumoniae

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant enzyme, hanging-drop or sitting-drop vapor diffusion, mixing of 10 mg/ml protein in 10 mM Tris-HCl, pH 7.0, with reservoir solution containing of 20% PEG 8000, 100 mM sodium cacodylate, pH 6.5, and 0.2 M zinc acetate, to a finaal volume of 0.01 ml, equilibration against 0.5 ml reservoir solution, 1 month, 16°C, X-ray diffraction structure determination and analysis at 1.54 A resolution, modeling and molecular replacement Klebsiella pneumoniae

Inhibitors

Inhibitors Comment Organism Structure
aztreonam
-
Klebsiella pneumoniae
additional information no inhibition by clavulanic acid Klebsiella pneumoniae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
cefepime + H2O Klebsiella pneumoniae
-
?
-
?
cefepime + H2O Klebsiella pneumoniae NU2936
-
?
-
?
cephalothin + H2O Klebsiella pneumoniae
-
?
-
?
cephalothin + H2O Klebsiella pneumoniae NU2936
-
?
-
?
additional information Klebsiella pneumoniae the enzyme hydrolyzes penicillins, cephalothin, and the expanded-spectrum cephalosporins cefepime and moxalactam ?
-
?
additional information Klebsiella pneumoniae NU2936 the enzyme hydrolyzes penicillins, cephalothin, and the expanded-spectrum cephalosporins cefepime and moxalactam ?
-
?
moxalactam + H2O Klebsiella pneumoniae
-
?
-
?
moxalactam + H2O Klebsiella pneumoniae NU2936
-
?
-
?

Organism

Organism UniProt Comment Textmining
Klebsiella pneumoniae Q51578 mox1, plasmid-encoded
-
Klebsiella pneumoniae NU2936 Q51578 mox1, plasmid-encoded
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli BL21(DE3)/pLysS by nickel affinity chhromatography and gel filtration Klebsiella pneumoniae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cefepime + H2O
-
Klebsiella pneumoniae ?
-
?
cefepime + H2O
-
Klebsiella pneumoniae NU2936 ?
-
?
cefepime + H2O
-
Klebsiella pneumoniae (2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
?
cefepime + H2O
-
Klebsiella pneumoniae NU2936 (2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
?
cephalothin + H2O
-
Klebsiella pneumoniae ?
-
?
cephalothin + H2O
-
Klebsiella pneumoniae NU2936 ?
-
?
cephalothin + H2O
-
Klebsiella pneumoniae (2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
?
additional information the enzyme hydrolyzes penicillins, cephalothin, and the expanded-spectrum cephalosporins cefepime and moxalactam Klebsiella pneumoniae ?
-
?
additional information the enzyme hydrolyzes penicillins, cephalothin, and the expanded-spectrum cephalosporins cefepime and moxalactam Klebsiella pneumoniae NU2936 ?
-
?
moxalactam + H2O
-
Klebsiella pneumoniae ?
-
?
moxalactam + H2O
-
Klebsiella pneumoniae NU2936 ?
-
?

Subunits

Subunits Comment Organism
More three-dimensional structure, overview Klebsiella pneumoniae

Synonyms

Synonyms Comment Organism
class C beta-lactamase
-
Klebsiella pneumoniae
Mox-1
-
Klebsiella pneumoniae
Mox-1 beta-lactamase
-
Klebsiella pneumoniae

General Information

General Information Comment Organism
additional information Mox-1 is a unique plasmid-mediated class C beta-lactamase. Structure comparison with other beta-lactamases shows that two region in Mox 1, amino acid residues 214 to 216 positioned in the omega loop and the other in the N-terminus of the B3 beta-strand corresponding to amino acid residues 303 to 306, having significant structural flexibility of these regions, may impact the recognition and binding of substrates in Mox-1 leading to the unique substrate profile of the enzyme, overview. A substrate-induced conformational change underlies the basis of the hydrolytic profile of Mox-1 beta-lactamase, active site structure of enzyme Mox-1, overview Klebsiella pneumoniae