Exploring the role of L10 loop in New Delhi metallo-β-lactamase (NDM-1): Kinetic and dynamic studies
A Piccirilli, E Criscuolo, F Brisdelli, PS Mercuri… - Molecules, 2021 - mdpi.com
Four NDM-1 mutants (L218T, L221T, L269H and L221T/Y229W) were generated in order to
investigate the role of leucines positioned in L10 loop. A detailed kinetic analysis stated that …
investigate the role of leucines positioned in L10 loop. A detailed kinetic analysis stated that …
Kinetic profile and molecular dynamic studies show that Y229W substitution in an NDM-1/L209F variant restores the hydrolytic activity of the enzyme toward penicillins …
A Piccirilli, F Brisdelli, M Aschi, G Celenza… - Antimicrobial Agents …, 2019 - Am Soc Microbiol
ABSTRACT The New Delhi metallo-β-lactamase-1 (NDM-1) enzyme is the most common
metallo-β-lactamase identified in many Gram-negative bacteria causing severe nosocomial …
metallo-β-lactamase identified in many Gram-negative bacteria causing severe nosocomial …
Exploring the role of L209 residue in the active site of NDM-1 a metallo-β-lactamase
Background New Delhi Metallo-β-Lactamase (NDM-1) is one of the most recent additions to
the β-lactamases family. Since its discovery in 2009, NDM-1 producing Enterobacteriaceae …
the β-lactamases family. Since its discovery in 2009, NDM-1 producing Enterobacteriaceae …
Role of non-active site residues in maintaining New Delhi metallo-β-lactamase-1 (NDM-1) function: an approach of site-directed mutagenesis and docking
New Delhi metallo-β-lactamase-1 (NDM-1) has been known to hydrolyze nearly all β-lactam
antibiotics, leading to a multidrug-resistant state. Hence, it is important to study its structure …
antibiotics, leading to a multidrug-resistant state. Hence, it is important to study its structure …
Flexible loops of New Delhi metallo-β-lactamase modulate its activity towards different substrates
JE Raczynska, B Imiolczyk, M Komorowska… - International journal of …, 2020 - Elsevier
Two accessory loop regions that are present in numerous variants of New Delhi metallo-β-
lactamases (NDM) are important for the enzymatic activity. The first one is a flexible loop L3 …
lactamases (NDM) are important for the enzymatic activity. The first one is a flexible loop L3 …
Molecular mechanisms of substrate recognition and specificity of New Delhi metallo-β-lactamase
J Chiou, TYC Leung, S Chen - Antimicrobial agents and …, 2014 - Am Soc Microbiol
Carbapenems are one of the last lines of defense for Gram-negative pathogens, such as
members of the Enterobacteriaceae. Despite the fact that most carbapenems are resistant to …
members of the Enterobacteriaceae. Despite the fact that most carbapenems are resistant to …
Non-active site mutation (Q123A) in New Delhi metallo-β-lactamase (NDM-1) enhanced its enzyme activity
New Delhi metallo β-lactamase-1 is one of the carbapenemases, causing hydrolysis of
almost all β-lactamase antibiotics. Seventeen different NDM variants have been reported so …
almost all β-lactamase antibiotics. Seventeen different NDM variants have been reported so …
E152A substitution drastically affects NDM-5 activity
Abstract New Delhi Metallo beta-lactamase (NDM) is of significant public health concern due
to its enormous potential to hydrolyse all major beta-lactams including carbapenems. Amino …
to its enormous potential to hydrolyse all major beta-lactams including carbapenems. Amino …
Role of non-active-site residue Trp-93 in the function and stability of New Delhi metallo-β-lactamase 1
New Delhi metallo-β-lactamase-1 (NDM-1) is expressed by various members of
Enterobacteriaceae as a defense mechanism to hydrolyze β-lactam antibiotics. Despite …
Enterobacteriaceae as a defense mechanism to hydrolyze β-lactam antibiotics. Despite …
Glutamic acid at position 152 and serine at position 191 are key residues required for the metallo-β-lactamase activity of NDM-7
New Delhi metallo-β-lactamase (NDM) is of significant public-health concern due to its
enormous potential to hydrolyse all of the major β-lactams, including carbapenems …
enormous potential to hydrolyse all of the major β-lactams, including carbapenems …
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