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Literature summary for 3.5.2.6 extracted from

  • Garcia-Saez, I.; Hopkins, J.; Papamicael, C.; Franceschini, N.; Amicosante, G.; Rossolini, G.M.; Galleni, M.; Frere, J.M.; Dideberg, O.
    The 1.5-A structure of Chryseobacterium meningosepticum zinc beta-lactamase in complex with the inhibitor, D-captopril (2003), J. Biol. Chem., 278, 23868-23873.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
enzyme BlaB in complex with the inhibitor D-captopril, hanging drop method, 0.002 ml of 5 mg/ml protein in 10 mM sodium cacodylate, 0.1 mM zinc acetate, 0.1 mM DTT, pH 6.5, is mixed with 0.001 ml of reservoir solution containing 28% PEG 4000, 0.2 M sodium acetate, 0.1 M Tris-HCl, pH 8.4, at 8°C, 3 weeks, complexing by soaking of the crystals in a solution containing 2 mM D-captopril for 5 weeks, cryoprotection by 15% glycerol, X-ray diffraction structure determination and analysis at 1.5 A resolution Elizabethkingia meningoseptica

Inhibitors

Inhibitors Comment Organism Structure
D-captopril acts by displacing the catalytic hydroxyl ion required for antibiotic hydrolysis and by intercalating its sulfhydryl group between the 2 Zn2+ ions, the inhibitor molecule is located on one side of the active site cleft Elizabethkingia meningoseptica

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ metalloenzyme, 2 Zn2+ binding sites Elizabethkingia meningoseptica

Organism

Organism UniProt Comment Textmining
Elizabethkingia meningoseptica
-
class B enzyme BlaB, subclass B1
-

Subunits

Subunits Comment Organism
More the enzyme shows a typical alphabeta/betaalpha metallo-beta-lactamase fold Elizabethkingia meningoseptica

Synonyms

Synonyms Comment Organism
BlaB
-
Elizabethkingia meningoseptica
zinc beta-lactamase
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Elizabethkingia meningoseptica