Substrate and Product-Assisted Catalysis: Molecular Aspects behind Structural Switches along Organic Hydroperoxide Resistance Protein Catalytic Cycle

ACS Catalysis ◽  
2020 ◽  
Vol 10 (12) ◽  
pp. 6587-6602
Author(s):  
Renato M. Domingos ◽  
Raphael D. Teixeira ◽  
Ari Zeida ◽  
William A. Agudelo ◽  
Thiago G. P. Alegria ◽  
...  
Keyword(s):  
Catalytic Cycle ◽  
Organic Hydroperoxide ◽  
Resistance Protein ◽  
Molecular Aspects

scholarly journals The Structure of the Organic Hydroperoxide Resistance Protein fromDeinococcus radiodurans

2004 ◽  
Vol 279 (24) ◽  
pp. 25830-25837 ◽  
Author(s):  
Cécile Meunier-Jamin ◽  
Ulrike Kapp ◽  
Gordon A. Leonard ◽  
Seán McSweeney
Keyword(s):  
Organic Hydroperoxide ◽  
Resistance Protein

scholarly journals Ohr (Organic Hydroperoxide Resistance Protein) Possesses a Previously Undescribed Activity, Lipoyl-dependent Peroxidase

2010 ◽  
Vol 285 (29) ◽  
pp. 21943-21950 ◽  
Author(s):  
José R. R. Cussiol ◽  
Thiago G. P. Alegria ◽  
Luke I. Szweda ◽  
Luis E. S. Netto
Keyword(s):  
Organic Hydroperoxide ◽  
Resistance Protein

scholarly journals Ohr (Organic hydroperoxide resistance protein) Possesses a Previously Undescribed Activity: Lipoyldependent Peroxidase

2010 ◽  
Vol 49 ◽  
pp. S164
Author(s):  
José Renato Rosa Cussiol ◽  
Thiago Geronimo Pires Alegria ◽  
Luke Ignatius Szweda ◽  
Luis Eduardo Soares Netto
Keyword(s):  
Organic Hydroperoxide ◽  
Resistance Protein

The mpn668 gene of Mycoplasma pneumoniae encodes a novel organic hydroperoxide resistance protein

2018 ◽  
Vol 308 (7) ◽  
pp. 776-783 ◽  
Author(s):  
Lie-Song Chen ◽  
Chun Li ◽  
Xiao-Xing You ◽  
Ying-Wu Lin ◽  
Yi-Mou Wu
Keyword(s):  
Mycoplasma Pneumoniae ◽  
Organic Hydroperoxide ◽  
Resistance Protein

Structural Insights into Enzyme–Substrate Interaction and Characterization of Enzymatic Intermediates of Organic Hydroperoxide Resistance Protein from Xylella fastidiosa

2006 ◽  
Vol 359 (2) ◽  
pp. 433-445 ◽  
Author(s):  
Marcos A. Oliveira ◽  
Beatriz G. Guimarães ◽  
José R.R. Cussiol ◽  
Francisco J. Medrano ◽  
Fábio C. Gozzo ◽  
...  
Keyword(s):  
Xylella Fastidiosa ◽  
Organic Hydroperoxide ◽  
Substrate Interaction ◽  
Enzyme Substrate ◽  
Resistance Protein ◽  
Structural Insights

scholarly journals Interaction of the Plasmid-Encoded Quinolone Resistance Protein Qnr with Escherichia coli DNA Gyrase

2005 ◽  
Vol 49 (1) ◽  
pp. 118-125 ◽  
Author(s):  
John H. Tran ◽  
George A. Jacoby ◽  
David C. Hooper
Keyword(s):  
Escherichia Coli ◽  
Dna Gyrase ◽  
Quinolone Resistance ◽  
Catalytic Cycle ◽  
Repeat Family ◽  
Biochemical Basis ◽  
Chromosomal Genes ◽  
Resistance Protein ◽  
Cleavage Complex ◽  
Gyrase Inhibitors

ABSTRACT Quinolone resistance normally arises by mutations in the chromosomal genes for type II topoisomerases and by changes in the expression of proteins that control the accumulation of quinolones inside bacteria. A novel mechanism of plasmid-mediated quinolone resistance was recently reported that involves DNA gyrase protection by a pentapeptide repeat family member called Qnr. This family includes two other members, McbG and MfpA, that are also involved in resistance to gyrase inhibitors. Purified Qnr-His6 was shown to protect Escherichia coli DNA gyrase directly from inhibition by ciprofloxacin. Here we have provided a biochemical basis for the mechanism of quinolone resistance. We have shown that Qnr can bind to the gyrase holoenzyme and its respective subunits, GyrA and GyrB. The binding of Qnr to gyrase does not require the presence of the complex of enzyme, DNA, and quinolone, since binding occurred in the absence of relaxed DNA, ciprofloxacin, or ATP. We hypothesize that the formation of Qnr-gyrase complex occurs before the formation of the cleavage complex. Furthermore, there was a decrease in DNA binding by gyrase when the enzyme interacted with Qnr. Therefore, it is possible that the reaction intermediate recognized by Qnr is one early in the gyrase catalytic cycle, in which gyrase has just begun to interact with DNA. Quinolones bind later in the catalytic cycle and stabilize a ternary complex consisting of the drug, gyrase, and DNA. By lowering gyrase binding to DNA, Qnr may reduce the amount of holoenzyme-DNA targets for quinolone inhibition.

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