NDM‐1, the ultimate promiscuous enzyme: substrate recognition and catalytic mechanism-Reference-Cited by-同舟云学术

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NDM‐1, the ultimate promiscuous enzyme: substrate recognition and catalytic mechanism

Published:2013-01-30 Issue:5 Volume:27 Page:1917-1927
ISSN:0892-6638
Container-title:The FASEB Journal
language:en
Short-container-title:FASEB j.

Author:

Kim Youngchang¹²,Cunningham Mark A.³,Mire Joseph⁴,Tesar Christine¹²,Sacchettini James⁴,Joachimiak Andrzej¹²

Affiliation:

1. Midwest Center for Structural GenomicsArgonne National LaboratoryArgonneIllinoisUSA

2. Structural Biology Center, Biosciences DivisionArgonne National LaboratoryArgonneIllinoisUSA

3. Department of Physics and GeologyUniversity of Texas–Pan AmericanEdinburgTexasUSA

4. Department of Biochemistry and BiophysicsTexas A&M UniversityCollege StationTexasUSA

Funder

Argonne National Laboratory

National Institutes of Health

U.S. Department of Energy

Publisher

Wiley

Subject

Genetics,Molecular Biology,Biochemistry,Biotechnology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1096/fj.12-224014

Reference44 articles.

1. Antibiotic resistance is ancient

2. Has the era of untreatable infections arrived?

3. Bacterial Resistance to β-Lactam Antibiotics: Compelling Opportunism, Compelling Opportunity

4. Updated Functional Classification of β-Lactamases

5. Emergence of a new antibiotic resistance mechanism in India, Pakistan, and the UK: a molecular, biological, and epidemiological study

Cited by 107 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Theoretical study of the hydrolysis mechanism of β -lactam antibiotics catalysed by a Zn(II) dinuclear biomimetic organometallic complex;Molecular Physics;2024-05-20

2. Interplay between the β-lactam side chain and an active-site mobile loop of NDM-1 in penicillin hydrolysis as a potential target for mechanism-based inhibitor design;International Journal of Biological Macromolecules;2024-03

3. The evosystem: A centerpiece for evolutionary studies;BioEssays;2024-02-12

4. Catalytic site flexibility facilitates the substrate and catalytic promiscuity of Vibrio dual lipase/transferase;Nature Communications;2023-08-09

5. A modified bonded model approach for molecular dynamics simulations of New Delhi Metallo-β-lactamase;Journal of Molecular Graphics and Modelling;2023-06

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