Glutathione Reductase Turned into Trypanothione Reductase:  Structural Analysis of an Engineered Change in Substrate Specificity†,‡

Biochemistry ◽  
1997 ◽  
Vol 36 (21) ◽  
pp. 6437-6447 ◽  
Author(s):  
Vincent S. Stoll ◽  
Sarah J. Simpson ◽  
R. Luise Krauth-Siegel ◽  
Christopher T. Walsh ◽  
Emil F. Pai
Keyword(s):  
Structural Analysis ◽  
Substrate Specificity ◽  
Glutathione Reductase ◽  
Trypanothione Reductase

scholarly journals The Metalloid Reductase of Pseudomonas Moravenis Stanleyae Conveys Nanoparticle Mediated Metalloid Tolerance

2018 ◽  
Author(s):  
Richard Nemeth ◽  
Mackenzie Neubert ◽  
Thomas Ni ◽  
Christopher J. Ackerson
Keyword(s):  
Structural Analysis ◽  
Substrate Specificity ◽  
Glutathione Reductase ◽  
Cell Lines ◽  
Bacterial Cell ◽  
Binding Pocket ◽  
Oxidized Glutathione ◽  
Se Nanoparticles ◽  
In Cells

In the present work we have identified a glutathione reductase like metalloid reductase (GRLMR) responsible for mediating selenite tolerance in <i>Pseudomonas moravenis</i> stanleyae through the enzymatic generation of Se(0) nanoparticles. This enzyme has an unprecedented substrate specificity for selenodiglutathione (K<sub>m</sub>= 336 μM) over oxidized glutathione (K<sub>m</sub>=8.22 mM). This enzyme was able to induce selenite tolerance in foreign bacterial cell lines by increasing the IC<sub>90</sub> for selenite from 1.9 mM in cell lacking the GRLMR gene to 21.3 mM for cells containing the GRLMR gene. It was later confirmed by STEM and EDS that Se nanoparticles were absent in control cells and present in cells expressing GRLMR. Structural analysis suggests the lack of a sulfur residue in the substrate/product binding pocket may be responsible for this unique substrate specificity.

scholarly journals The Metalloid Reductase of Pseudomonas Moravenis Stanleyae Conveys Nanoparticle Mediated Metalloid Tolerance

2018 ◽  
Author(s):  
Richard Nemeth ◽  
Mackenzie Neubert ◽  
Thomas Ni ◽  
Christopher J. Ackerson
Keyword(s):  
Structural Analysis ◽  
Substrate Specificity ◽  
Glutathione Reductase ◽  
Cell Lines ◽  
Bacterial Cell ◽  
Binding Pocket ◽  
Oxidized Glutathione ◽  
Se Nanoparticles ◽  
In Cells

In the present work we have identified a glutathione reductase like metalloid reductase (GRLMR) responsible for mediating selenite tolerance in <i>Pseudomonas moravenis</i> stanleyae through the enzymatic generation of Se(0) nanoparticles. This enzyme has an unprecedented substrate specificity for selenodiglutathione (K<sub>m</sub>= 336 μM) over oxidized glutathione (K<sub>m</sub>=8.22 mM). This enzyme was able to induce selenite tolerance in foreign bacterial cell lines by increasing the IC<sub>90</sub> for selenite from 1.9 mM in cell lacking the GRLMR gene to 21.3 mM for cells containing the GRLMR gene. It was later confirmed by STEM and EDS that Se nanoparticles were absent in control cells and present in cells expressing GRLMR. Structural analysis suggests the lack of a sulfur residue in the substrate/product binding pocket may be responsible for this unique substrate specificity.

scholarly journals Biochemical and Structural Analysis of Substrate Specificity of a Phenylalanine Ammonia-Lyase

2017 ◽  
Vol 176 (2) ◽  
pp. 1452-1468 ◽  
Author(s):  
Se-Young Jun ◽  
Steven A. Sattler ◽  
Gabriel S. Cortez ◽  
Wilfred Vermerris ◽  
Scott E. Sattler ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Substrate Specificity ◽  
Phenylalanine Ammonia Lyase

scholarly journals A comparative structural analysis reveals distinctive features of co-factor binding and substrate specificity in plant aldo-keto reductases

2016 ◽  
Vol 474 (4) ◽  
pp. 696-701 ◽  
Author(s):  
Priscila Oliveira de Giuseppe ◽  
Marcelo Leite dos Santos ◽  
Sylvia Morais de Sousa ◽  
Karen E. Koch ◽  
José Andrés Yunes ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Substrate Specificity ◽  
Distinctive Features ◽  
Factor Binding

Leishmania infantum trypanothione reductase is a promiscuous enzyme carrying an NADPH:O2 oxidoreductase activity shared by glutathione reductase

2015 ◽  
Vol 1850 (9) ◽  
pp. 1891-1897 ◽  
Author(s):  
Gabriella Angiulli ◽  
Antonella Lantella ◽  
Elena Forte ◽  
Francesco Angelucci ◽  
Gianni Colotti ◽  
...  
Keyword(s):  
Glutathione Reductase ◽  
Leishmania Infantum ◽  
Trypanothione Reductase ◽  
Oxidoreductase Activity

scholarly journals Structural Analysis of Glutaredoxin Domain of Mus musculus Thioredoxin Glutathione Reductase

PLoS ONE ◽  
2012 ◽  
Vol 7 (12) ◽  
pp. e52914 ◽  
Author(s):  
Olena Dobrovolska ◽  
Elena Shumilina ◽  
Vadim N. Gladyshev ◽  
Alexander Dikiy
Keyword(s):  
Structural Analysis ◽  
Glutathione Reductase ◽  
Mus Musculus ◽  
Thioredoxin Glutathione Reductase

scholarly journals Structural Analysis ofXanthomonasXopD Provides Insights into Substrate Specificity of Ubiquitin-like Protein Proteases

2007 ◽  
Vol 282 (9) ◽  
pp. 6773-6782 ◽  
Author(s):  
Renee Chosed ◽  
Diana R. Tomchick ◽  
Chad A. Brautigam ◽  
Sohini Mukherjee ◽  
Veera S. Negi ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Substrate Specificity
Sign in / Sign up

Export Citation Format

Share Document