New Delhi metallo-β-lactamase: structural insights into β-lactam recognition and inhibition

DT King, LJ Worrall, R Gruninger… - Journal of the American …, 2012 - ACS Publications
The β-lactam antibiotics have long been a cornerstone for the treatment of bacterial disease.
Recently, a readily transferable antibiotic resistance factor called the New Delhi metallo-β …

Structure of apo-and monometalated forms of NDM-1—a highly potent carbapenem-hydrolyzing metallo-β-lactamase

Y Kim, C Tesar, J Mire, R Jedrzejczak, A Binkowski… - PloS one, 2011 - journals.plos.org
The New Delhi Metallo-β-lactamase (NDM-1) gene makes multiple pathogenic
microorganisms resistant to all known β-lactam antibiotics. The rapid emergence of NDM-1 …

Crystal structure of New Delhi metallo‐β‐lactamase reveals molecular basis for antibiotic resistance

D King, N Strynadka - Protein Science, 2011 - Wiley Online Library
Abstract β‐Lactams are the most commonly prescribed class of antibiotics and have had an
enormous impact on human health. Thus, it is disquieting that an enzyme called New Delhi …

Ten years with New Delhi metallo-β-lactamase-1 (NDM-1): from structural insights to inhibitor design

P Linciano, L Cendron, E Gianquinto… - ACS infectious …, 2018 - ACS Publications
The worldwide emergence of New Delhi metallo-β-lactamase-1 (NDM-1) as a
carbapenemase able to hydrolyze nearly all available β-lactam antibiotics has characterized …

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

H Feng, X Liu, S Wang, J Fleming, DC Wang… - Nature …, 2017 - nature.com
New Delhi metallo-β-lactamases (NDMs), the recent additions to metallo-β-lactamases
(MBLs), pose a serious public health threat due to its highly efficient hydrolysis of β-lactam …

Insights from modeling the 3D structure of New Delhi metallo-β-lactamse and its binding interactions with antibiotic drugs

JF Wang, KC Chou - PLoS One, 2011 - journals.plos.org
New Delhi metallo-beta-lactamase (NDM-1) is an enzyme that makes bacteria resistant to a
broad range of beta-lactam antibiotic drugs. This is because it can inactivate most beta …

Metallo-β-lactamase: structure and mechanism

Z Wang, W Fast, AM Valentine, SJ Benkovic - Current opinion in chemical …, 1999 - Elsevier
This past year has produced determinations of X-ray crystal structures for three metallo-β-
lactamases and the elucidation of the catalytic mechanisms for a monozinc and a dizinc …

Crystal structure of NDM‐1 reveals a common β‐lactam hydrolysis mechanism

M Zhang, Q Hao - The FASEB Journal, 2011 - Wiley Online Library
ABSTRACT Metallo‐β‐lactamases (MBLs) hydrolyze most β‐lactam antibiotics, and bacteria
containing this kind of enzyme pose a serious threat to the public health. The newly …

[HTML][HTML] Overcoming differences: the catalytic mechanism of metallo-β-lactamases

MR Meini, LI Llarrull, AJ Vila - FEBS letters, 2015 - Elsevier
Metallo-β-lactamases are the latest resistance mechanism of pathogenic and opportunistic
bacteria against carbapenems, considered as last resort drugs. The worldwide spread of …

Antibiotic recognition by binuclear metallo-β-lactamases revealed by X-ray crystallography

J Spencer, J Read, RB Sessions, S Howell… - Journal of the …, 2005 - ACS Publications
Metallo-β-lactamases are zinc-dependent enzymes responsible for resistance to β-lactam
antibiotics in a variety of host bacteria, usually Gram-negative species that act as opportunist …