Structural highlights
Function
BLO10_PSEAI Hydrolyzes both carbenicillin and oxacillin.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The activity of class D beta-lactamases is dependent on Lys70 carboxylation in the active site. Structural, kinetic and affinity studies show that this post-translational modification can be affected by the presence of a poor substrate such as moxalactam but also by the V117T substitution. Val117 is a strictly conserved hydrophobic residue located in the active site. In addition, inhibition of class D beta-lactamases by chloride ions is due to a competition between the side chain carboxylate of the modified Lys70 and chloride ions. Determination of the individual kinetic constants shows that the deacylation of the acyl-enzyme is the rate-limiting step for the wild-type OXA-10 beta-lactamase.
Three factors that modulate the activity of class D beta-lactamases and interfere with the post-translational carboxylation of Lys70.,Vercheval L, Bauvois C, di Paolo A, Borel F, Ferrer JL, Sauvage E, Matagne A, Frere JM, Charlier P, Galleni M, Kerff F Biochem J. 2010 Nov 25;432(3):495-504. PMID:21108605[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Vercheval L, Bauvois C, di Paolo A, Borel F, Ferrer JL, Sauvage E, Matagne A, Frere JM, Charlier P, Galleni M, Kerff F. Three factors that modulate the activity of class D beta-lactamases and interfere with the post-translational carboxylation of Lys70. Biochem J. 2010 Nov 25;432(3):495-504. PMID:21108605 doi:10.1042/BJ20101122
