TY - JOUR
T1 - Neutron and X-ray crystal structures of a perdeuterated enzyme inhibitor complex reveal the catalytic proton network of the Toho-1 β-lactamase for the acylation reaction
AU - Tomanicek, Stephen J.
AU - Standaert, Robert F.
AU - Weiss, Kevin L.
AU - Ostermann, Andreas
AU - Schrader, Tobias E.
AU - Ng, Joseph D.
AU - Coates, Leighton
PY - 2013/2/15
Y1 - 2013/2/15
N2 - Background: Antibiotic resistance from extended-spectrum β-lactamases (ESBLs) makes infections more dangerous and difficult to treat. Results: Neutron and x-ray crystal structures were determined for an ESBL in complex with an acylation transition state analog. Conclusion: Glu-166 is implicated as the general base in the acylation reaction. Significance: Understanding the catalytic mechanism of β-lactamases will lead to improved antibiotics and β-lactamase inhibitors.
AB - Background: Antibiotic resistance from extended-spectrum β-lactamases (ESBLs) makes infections more dangerous and difficult to treat. Results: Neutron and x-ray crystal structures were determined for an ESBL in complex with an acylation transition state analog. Conclusion: Glu-166 is implicated as the general base in the acylation reaction. Significance: Understanding the catalytic mechanism of β-lactamases will lead to improved antibiotics and β-lactamase inhibitors.
UR - http://www.scopus.com/inward/record.url?scp=84874077280&partnerID=8YFLogxK
U2 - 10.1074/jbc.M112.436238
DO - 10.1074/jbc.M112.436238
M3 - Article
C2 - 23255594
AN - SCOPUS:84874077280
SN - 0021-9258
VL - 288
SP - 4715
EP - 4722
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 7
ER -