Purification and Substrate-Specificity of β-Xylosidase from Sycamore Cell (Acer-Pseudoplatanus L.): Application for Structural Analysis of Xylose-Containing N-Linked Oligosaccharides

1993 ◽  
Vol 211 (2) ◽  
pp. 205-209 ◽  
Author(s):  
K. Tezuka ◽  
M. Hayashi ◽  
H. Ishihara ◽  
M. Nishimura ◽  
K. Onozaki ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Substrate Specificity ◽  
Acer Pseudoplatanus

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

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 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

scholarly journals Structural Analysis of the Catalytic Mechanism and Substrate Specificity ofAnabaenaAlkaline Invertase InvA Reveals a Novel Glucosidase

2016 ◽  
Vol 291 (49) ◽  
pp. 25667-25677 ◽  
Author(s):  
Jin Xie ◽  
Kun Cai ◽  
Hai-Xi Hu ◽  
Yong-Liang Jiang ◽  
Feng Yang ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Substrate Specificity ◽  
Catalytic Mechanism

scholarly journals Structural Analysis ofSaccharomyces cerevisiaeα-Galactosidase and Its Complexes with Natural Substrates Reveals New Insights into Substrate Specificity of GH27 Glycosidases

2010 ◽  
Vol 285 (36) ◽  
pp. 28020-28033 ◽  
Author(s):  
Rafael Fernández-Leiro ◽  
Ángel Pereira-Rodríguez ◽  
M. Esperanza Cerdán ◽  
Manuel Becerra ◽  
Juliana Sanz-Aparicio
Keyword(s):  
Structural Analysis ◽  
Substrate Specificity

scholarly journals Kinetic and Structural Analysis of Substrate Specificity in Two Copper Amine Oxidases fromHansenula polymorpha

Biochemistry ◽  
2010 ◽  
Vol 49 (11) ◽  
pp. 2540-2550 ◽  
Author(s):  
Cindy M. Chang ◽  
Valerie J. Klema ◽  
Bryan J. Johnson ◽  
Minae Mure ◽  
Judith P. Klinman ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Substrate Specificity ◽  
Amine Oxidases ◽  
Copper Amine Oxidases ◽  
Copper Amine

scholarly journals Structural Analysis of Actinorhodin Polyketide Ketoreductase: Cofactor Binding and Substrate Specificity

2006 ◽  
Vol 20 (5) ◽  
Author(s):  
Tyler Korman ◽  
Jason Hill ◽  
Thanh Vu ◽  
Shiou‐Chuan Tsai
Keyword(s):  
Structural Analysis ◽  
Substrate Specificity ◽  
Cofactor Binding

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.

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