The metallo-beta-lactamase protein fold is a protein domain contained in class B beta-lactamases and a number of other proteins . These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.
Metallo-beta-lactamases are important enzymes because they are involved in the breakdown of antibiotics by antibiotic-resistant bacteria.
- ^ a b PDB 1bmc ; Carfi A, Pares S, Duée E, Galleni M, Duez C, Frère JM, Dideberg O (October 1995). "The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold". EMBO J. 14 (20): 4914–21. PMC 394593. PMID 7588620.
- ^ "Shaw, Robert W. (Lubbock, TX, US), Kim, Sung-kun (Lubbock, TX, US)" ("November" "2008"). "Inhibition of metallo-β-lactamase" ("7456274").
This article incorporates text from the public domain Pfam and InterPro IPR001279