Literature DB >> 9401719

Inhibition of the metallo-beta-lactamase produced from Serratia marcescens by thiol compounds.

M Goto1, T Takahashi, F Yamashita, A Koreeda, H Mori, M Ohta, Y Arakawa.   

Abstract

Low molecular weight thiol compounds have been found to be strong inhibitors of metallo-beta-lactamase (IMP-1) produced by Serratia marcescens TN9106, which was expressed by Echerichia coli JM109 cells. Mercaptoacetic acid and 2-mercaptopropionic acid strongly and competitively inhibited IMP-1 with Ki of 0.23 and 0.19 microM, respectively. 2-Mercaptoethanol reversibly inhibited IMP-1 but did not show simple competitive inhibition.

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Year:  1997        PMID： 9401719     DOI： 10.1248/bpb.20.1136

Source DB:  PubMed          Journal:  Biol Pharm Bull        ISSN： 0918-6158            Impact factor:   2.233


  9 in total

1.  The cysteine dioxygenase homologue from Pseudomonas aeruginosa is a 3-mercaptopropionate dioxygenase.

Authors:  Egor P Tchesnokov; Matthias Fellner; Eleni Siakkou; Torsten Kleffmann; Lois W Martin; Sekotilani Aloi; Iain L Lamont; Sigurd M Wilbanks; Guy N L Jameson
Journal:  J Biol Chem       Date:  2015-08-13       Impact factor: 5.157

Review 2.  A close look onto structural models and primary ligands of metallo-β-lactamases.

Authors:  Joanna E Raczynska; Ivan G Shabalin; Wladek Minor; Alexander Wlodawer; Mariusz Jaskolski
Journal:  Drug Resist Updat       Date:  2018-08-25       Impact factor: 18.500

3.  Convenient test for screening metallo-beta-lactamase-producing gram-negative bacteria by using thiol compounds.

Authors:  Y Arakawa; N Shibata; K Shibayama; H Kurokawa; T Yagi; H Fujiwara; M Goto
Journal:  J Clin Microbiol       Date:  2000-01       Impact factor: 5.948

Review 4.  Metallo-beta-lactamases: the quiet before the storm?

Authors:  Timothy R Walsh; Mark A Toleman; Laurent Poirel; Patrice Nordmann
Journal:  Clin Microbiol Rev       Date:  2005-04       Impact factor: 26.132

5.  N-arylsulfonyl hydrazones as inhibitors of IMP-1 metallo-beta-lactamase.

Authors:  Stefan Siemann; Darryl P Evanoff; Laura Marrone; Anthony J Clarke; Thammaiah Viswanatha; Gary I Dmitrienko
Journal:  Antimicrob Agents Chemother       Date:  2002-08       Impact factor: 5.191

6.  Structural insights into the subclass B3 metallo-β-lactamase SMB-1 and the mode of inhibition by the common metallo-β-lactamase inhibitor mercaptoacetate.

Authors:  Jun-Ichi Wachino; Yoshihiro Yamaguchi; Shigetarou Mori; Hiromasa Kurosaki; Yoshichika Arakawa; Keigo Shibayama
Journal:  Antimicrob Agents Chemother       Date:  2012-10-15       Impact factor: 5.191

Review 7.  Diversity and Proliferation of Metallo-β-Lactamases: a Clarion Call for Clinically Effective Metallo-β-Lactamase Inhibitors.

Authors:  Anou M Somboro; John Osei Sekyere; Daniel G Amoako; Sabiha Y Essack; Linda A Bester
Journal:  Appl Environ Microbiol       Date:  2018-08-31       Impact factor: 4.792

8.  Solution structures of the Bacillus cereus metallo-β-lactamase BcII and its complex with the broad spectrum inhibitor R-thiomandelic acid.

Authors:  Andreas Ioannis Karsisiotis; Christian F Damblon; Gordon C K Roberts
Journal:  Biochem J       Date:  2013-12-15       Impact factor: 3.857

9.  Synthesis and enzyme-based evaluation of analogues L-tyrosine thiol carboxylic acid inhibitor of metallo-β-lactamase IMP-1.

Authors:  Omid Khalili Arjomandi; Mahboubeh Kavoosi; Hadi Adibi
Journal:  J Enzyme Inhib Med Chem       Date:  2019-12       Impact factor: 5.051
  9 in total

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