The mechanism of NDM-1-catalyzed carbapenem hydrolysis is distinct from that of penicillin or cephalosporin hydrolysis

The mechanism of NDM-1-catalyzed carbapenem hydrolysis is distinct from that of penicillin or cephalosporin hydrolysis

New Delhi metallo-β-lactamases (NDMs) hydrolyze almost all β-lactam antibiotics and pose a major public health threat. Here, the authors study the mechanism of NDM-1 catalyzed carbapenem hydrolysis and present the crystal structures of the enzyme-intermediate and product complexes, which is importan...

Full description

Bibliographic Details
Main Authors: Han Feng, Xuehui Liu, Sheng Wang, Joy Fleming, Da-Cheng Wang, Wei Liu
Format: Article
Language:English
Published: Nature Publishing Group 2017-12-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-017-02339-w
id doaj-3d6920df3c794045acc9dd9cd1b32ccc
record_format Article
spelling doaj-3d6920df3c794045acc9dd9cd1b32ccc2021-05-11T07:30:57ZengNature Publishing GroupNature Communications2041-17232017-12-018111110.1038/s41467-017-02339-wThe mechanism of NDM-1-catalyzed carbapenem hydrolysis is distinct from that of penicillin or cephalosporin hydrolysisHan Feng0Xuehui Liu1Sheng Wang2Joy Fleming3Da-Cheng Wang4Wei Liu5National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of SciencesNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of SciencesKey Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and TechnologyKey Laboratory of RNA Biology, Institute of Biophysics, Chinese Academy of SciencesNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of SciencesInstitute of Immunology, The Third Military Medical UniversityNew Delhi metallo-β-lactamases (NDMs) hydrolyze almost all β-lactam antibiotics and pose a major public health threat. Here, the authors study the mechanism of NDM-1 catalyzed carbapenem hydrolysis and present the crystal structures of the enzyme-intermediate and product complexes, which is important for drug design.https://doi.org/10.1038/s41467-017-02339-w
collection DOAJ
language English
format Article
sources DOAJ
author Han Feng
Xuehui Liu
Sheng Wang
Joy Fleming
Da-Cheng Wang
Wei Liu
spellingShingle Han Feng
Xuehui Liu
Sheng Wang
Joy Fleming
Da-Cheng Wang
Wei Liu
The mechanism of NDM-1-catalyzed carbapenem hydrolysis is distinct from that of penicillin or cephalosporin hydrolysis
Nature Communications
author_facet Han Feng
Xuehui Liu
Sheng Wang
Joy Fleming
Da-Cheng Wang
Wei Liu
author_sort Han Feng
title The mechanism of NDM-1-catalyzed carbapenem hydrolysis is distinct from that of penicillin or cephalosporin hydrolysis
title_short The mechanism of NDM-1-catalyzed carbapenem hydrolysis is distinct from that of penicillin or cephalosporin hydrolysis
title_full The mechanism of NDM-1-catalyzed carbapenem hydrolysis is distinct from that of penicillin or cephalosporin hydrolysis
title_fullStr The mechanism of NDM-1-catalyzed carbapenem hydrolysis is distinct from that of penicillin or cephalosporin hydrolysis
title_full_unstemmed The mechanism of NDM-1-catalyzed carbapenem hydrolysis is distinct from that of penicillin or cephalosporin hydrolysis
title_sort mechanism of ndm-1-catalyzed carbapenem hydrolysis is distinct from that of penicillin or cephalosporin hydrolysis
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2017-12-01
description New Delhi metallo-β-lactamases (NDMs) hydrolyze almost all β-lactam antibiotics and pose a major public health threat. Here, the authors study the mechanism of NDM-1 catalyzed carbapenem hydrolysis and present the crystal structures of the enzyme-intermediate and product complexes, which is important for drug design.
url https://doi.org/10.1038/s41467-017-02339-w
work_keys_str_mv AT hanfeng themechanismofndm1catalyzedcarbapenemhydrolysisisdistinctfromthatofpenicillinorcephalosporinhydrolysis
AT xuehuiliu themechanismofndm1catalyzedcarbapenemhydrolysisisdistinctfromthatofpenicillinorcephalosporinhydrolysis
AT shengwang themechanismofndm1catalyzedcarbapenemhydrolysisisdistinctfromthatofpenicillinorcephalosporinhydrolysis
AT joyfleming themechanismofndm1catalyzedcarbapenemhydrolysisisdistinctfromthatofpenicillinorcephalosporinhydrolysis
AT dachengwang themechanismofndm1catalyzedcarbapenemhydrolysisisdistinctfromthatofpenicillinorcephalosporinhydrolysis
AT weiliu themechanismofndm1catalyzedcarbapenemhydrolysisisdistinctfromthatofpenicillinorcephalosporinhydrolysis
AT hanfeng mechanismofndm1catalyzedcarbapenemhydrolysisisdistinctfromthatofpenicillinorcephalosporinhydrolysis
AT xuehuiliu mechanismofndm1catalyzedcarbapenemhydrolysisisdistinctfromthatofpenicillinorcephalosporinhydrolysis
AT shengwang mechanismofndm1catalyzedcarbapenemhydrolysisisdistinctfromthatofpenicillinorcephalosporinhydrolysis
AT joyfleming mechanismofndm1catalyzedcarbapenemhydrolysisisdistinctfromthatofpenicillinorcephalosporinhydrolysis
AT dachengwang mechanismofndm1catalyzedcarbapenemhydrolysisisdistinctfromthatofpenicillinorcephalosporinhydrolysis
AT weiliu mechanismofndm1catalyzedcarbapenemhydrolysisisdistinctfromthatofpenicillinorcephalosporinhydrolysis
_version_ 1721452113327816704

Similar Items