Structural highlights
Function
BLT1_ECOLX Has strong cefotaxime-hydrolyzing activity.
Publication Abstract from PubMed
The mechanism by which class A beta-lactamase enzymes form an acyl-enzyme intermediate has been the emphasis of several studies. Here, we report on the use of neutron and high resolution X-ray diffraction to help elucidate the identity of the catalytic base in the acylation part of the mechanism.
Neutron and X-ray crystal structures of a perdeuterated enzyme inhibitor complex reveal the catalytic proton network of the Toho-1 beta-lactamase for the acylation reaction.,Tomanicek SJ, Standaert RF, Weiss KL, Ostermann A, Schrader TE, Ng JD, Coates L J Biol Chem. 2012 Dec 18. PMID:23255594[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tomanicek SJ, Standaert RF, Weiss KL, Ostermann A, Schrader TE, Ng JD, Coates L. Neutron and X-ray crystal structures of a perdeuterated enzyme inhibitor complex reveal the catalytic proton network of the Toho-1 beta-lactamase for the acylation reaction. J Biol Chem. 2012 Dec 18. PMID:23255594 doi:http://dx.doi.org/10.1074/jbc.M112.436238
