Structural highlights
Function
[BLKPC_KLEPN] Hydrolyzes carbapenems, penicillins, cephalosporins and monobactams with varying efficiency.
Publication Abstract from PubMed
Carbapenem-resistant Enterobacteriaceae are resistant to most beta-lactam antibiotics due to the production of the Klebsiella pneumoniae carbapenemase (KPC-2) class A beta-lactamase. Here, we present the first product complex crystal structures of KPC-2 with beta-lactam antibiotics containing hydrolyzed cefotaxime and faropenem. They provide experimental insights into substrate recognition by KPC-2 and its unique cephalosporinase/carbapenemase activity. These structures also represent the first product complexes for a wild-type serine beta-lactamase, elucidating the product release mechanism of these enzymes in general.
Molecular Basis of Substrate Recognition and Product Release by the Klebsiella pneumoniae Carbapenemase (KPC-2).,Pemberton OA, Zhang X, Chen Y J Med Chem. 2017 Apr 17. doi: 10.1021/acs.jmedchem.7b00158. PMID:28388065[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pemberton OA, Zhang X, Chen Y. Molecular Basis of Substrate Recognition and Product Release by the Klebsiella pneumoniae Carbapenemase (KPC-2). J Med Chem. 2017 Apr 17. doi: 10.1021/acs.jmedchem.7b00158. PMID:28388065 doi:http://dx.doi.org/10.1021/acs.jmedchem.7b00158
