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...
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 |
Similar Items
-
Differential active site requirements for NDM-1 β-lactamase hydrolysis of carbapenem versus penicillin and cephalosporin antibiotics
by: Zhizeng Sun, et al.
Published: (2018-10-01) -
A Study on Hydrolysis of Penicillin Catalyzed by Penicillin Acylase
by: Wang, Sung-Shyong, et al. -
The kinetics of the #beta#-lactamase catalysed hydrolysis of cephalosporins
by: Buckwell, S. C.
Published: (1987) -
Fractionation of the mixture obtained by the enzymatic hydrolysis of penicillin G
by: Cascaval Dan, et al.
Published: (2002-01-01) -
Structural analysis of Zn-Zn distance in NDM-1's beta-lactam hydrolysis mechanism
by: Hui, Ka-long, Aaron, et al.
Published: (2014)