Literature DB >> 26856833

Kinetic Study of Laboratory Mutants of NDM-1 Metallo-β-Lactamase and the Importance of an Isoleucine at Position 35.

Francesca Marcoccia1, Carlo Bottoni1, Alessia Sabatini1, Martina Colapietro1, Paola Sandra Mercuri2, Moreno Galleni2, Frédéric Kerff3, André Matagne4, Giuseppe Celenza1, Gianfranco Amicosante1, Mariagrazia Perilli5.   

Abstract

Two laboratory mutants of NDM-1 were generated by replacing the isoleucine at position 35 with threonine and serine residues: the NDM-1(I35T)and NDM-1(I35S)enzymes. These mutants were well characterized, and their kinetic parameters were compared with those of the NDM-1 wild type. Thekcat,Km, andkcat/Kmvalues calculated for the two mutants were slightly different from those of the wild-type enzyme. Interestingly, thekcat/Kmof NDM-1(I35S)for loracarbef was about 14-fold higher than that of NDM-1. Far-UV circular dichroism (CD) spectra of NDM-1 and NDM-1(I35T)and NDM-1(I35S)enzymes suggest local structural rearrangements in the secondary structure with a marked reduction of α-helix content in the mutants.
Copyright © 2016, American Society for Microbiology. All Rights Reserved.

Entities:  

Mesh：

Substances：

Year:  2016        PMID： 26856833      PMCID： PMC4808226          DOI： 10.1128/AAC.00531-15

Source DB:  PubMed          Journal:  Antimicrob Agents Chemother        ISSN： 0066-4804            Impact factor:   5.191


  31 in total

1.  DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data.

Authors:  Lee Whitmore; B A Wallace
Journal:  Nucleic Acids Res       Date:  2004-07-01       Impact factor: 16.971

2.  Estimation of the number of alpha-helical and beta-strand segments in proteins using circular dichroism spectroscopy.

Authors:  N Sreerama; S Y Venyaminov; R W Woody
Journal:  Protein Sci       Date:  1999-02       Impact factor: 6.725

3.  Making optimal use of empirical energy functions: force-field parameterization in crystal space.

Authors:  Elmar Krieger; Tom Darden; Sander B Nabuurs; Alexei Finkelstein; Gert Vriend
Journal:  Proteins       Date:  2004-12-01

4.  Automated analysis of enzyme inactivation phenomena. Application to beta-lactamases and DD-peptidases.

Authors:  F De Meester; B Joris; G Reckinger; C Bellefroid-Bourguignon; J M Frère; S G Waley
Journal:  Biochem Pharmacol       Date:  1987-07-15       Impact factor: 5.858

5.  Complete sequencing of an IncHI1 plasmid encoding the carbapenemase NDM-1, the ArmA 16S RNA methylase and a resistance-nodulation-cell division/multidrug efflux pump.

Authors:  Monika Dolejska; Laura Villa; Laurent Poirel; Patrice Nordmann; Alessandra Carattoli
Journal:  J Antimicrob Chemother       Date:  2012-09-11       Impact factor: 5.790

6.  Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

Authors:  U K Laemmli
Journal:  Nature       Date:  1970-08-15       Impact factor: 49.962

7.  Estimation of globular protein secondary structure from circular dichroism.

Authors:  S W Provencher; J Glöckner
Journal:  Biochemistry       Date:  1981-01-06       Impact factor: 3.162

8.  A self-consistent method for the analysis of protein secondary structure from circular dichroism.

Authors:  N Sreerama; R W Woody
Journal:  Anal Biochem       Date:  1993-02-15       Impact factor: 3.365

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

Authors:  Youngchang Kim; Christine Tesar; Joseph Mire; Robert Jedrzejczak; Andrew Binkowski; Gyorgy Babnigg; James Sacchettini; Andrzej Joachimiak
Journal:  PLoS One       Date:  2011-09-08       Impact factor: 3.240

10.  Evolution of Metallo-β-lactamases: Trends Revealed by Natural Diversity and in vitro Evolution.

Authors:  María-Rocío Meini; Leticia I Llarrull; Alejandro J Vila
Journal:  Antibiotics (Basel)       Date:  2014-07-01
View more
  9 in total

1.  A Kinetic Study of the Replacement by Site Saturation Mutagenesis of Residue 119 in NDM-1 Metallo-β-Lactamase.

Authors:  Francesca Marcoccia; Paola Sandra Mercuri; Moreno Galleni; Giuseppe Celenza; Gianfranco Amicosante; Mariagrazia Perilli
Journal:  Antimicrob Agents Chemother       Date:  2018-07-27       Impact factor: 5.191

2.  Active-Site Conformational Fluctuations Promote the Enzymatic Activity of NDM-1.

Authors:  Hongmin Zhang; Guixing Ma; Yifan Zhu; Lingxiao Zeng; Ashfaq Ahmad; Changzhi Wang; Bo Pang; Huiyan Fang; Liqing Zhao; Quan Hao
Journal:  Antimicrob Agents Chemother       Date:  2018-10-24       Impact factor: 5.191

3.  Kinetics of Sulbactam Hydrolysis by β-Lactamases, and Kinetics of β-Lactamase Inhibition by Sulbactam.

Authors:  Adam B Shapiro
Journal:  Antimicrob Agents Chemother       Date:  2017-11-22       Impact factor: 5.191

4.  Structure-Based Virtual Screening for the Discovery of Novel Inhibitors of New Delhi Metallo-β-lactamase-1.

Authors:  Francesca Spyrakis; Giuseppe Celenza; Francesca Marcoccia; Matteo Santucci; Simon Cross; Pierangelo Bellio; Laura Cendron; Mariagrazia Perilli; Donatella Tondi
Journal:  ACS Med Chem Lett       Date:  2017-11-26       Impact factor: 4.345

5.  Kinetic and Structural Characterization of the First B3 Metallo-β-Lactamase with an Active-Site Glutamic Acid.

Authors:  Liam A Wilson; Esmée G Knaven; Marc T Morris; Marcelo Monteiro Pedroso; Christopher J Schofield; Thomas B Brück; Mikael Boden; David W Waite; Philip Hugenholtz; Luke Guddat; Gerhard Schenk
Journal:  Antimicrob Agents Chemother       Date:  2021-07-26       Impact factor: 5.191

6.  Detection of carbapenemase producing enterobacteria using an ion sensitive field effect transistor sensor.

Authors:  Stathis D Kotsakis; Georgios Miliotis; Eva Tzelepi; Leonidas S Tzouvelekis; Vivi Miriagou
Journal:  Sci Rep       Date:  2021-06-08       Impact factor: 4.379

7.  Exploring the role of L209 residue in the active site of NDM-1 a metallo-β-lactamase.

Authors:  Francesca Marcoccia; Hanna-Kirsti S Leiros; Massimiliano Aschi; Gianfranco Amicosante; Mariagrazia Perilli
Journal:  PLoS One       Date:  2018-01-02       Impact factor: 3.240

8.  Direct Colorimetry of Imipenem Decomposition as a Novel Cost-Effective Method for Detecting Carbapenemase-Producing Enterobacteria.

Authors:  Stathis D Kotsakis; Anastasia Lambropoulou; Georgios Miliotis; Eva Tzelepi; Vivi Miriagou; Leonidas S Tzouvelekis
Journal:  Microbiol Spectr       Date:  2022-07-19

9.  Exploring the Role of L10 Loop in New Delhi Metallo-β-lactamase (NDM-1): Kinetic and Dynamic Studies.

Authors:  Alessandra Piccirilli; Emanuele Criscuolo; Fabrizia Brisdelli; Paola Sandra Mercuri; Sabrina Cherubini; Maria Laura De Sciscio; Mauro Maccarrone; Moreno Galleni; Gianfranco Amicosante; Mariagrazia Perilli
Journal:  Molecules       Date:  2021-09-09       Impact factor: 4.411
  9 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.