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 Phenylalanine, Tyrosine, and DOPA Are Bona Fide Substrates for Bambusa oldhamii BoPAL4

Catalysts ◽  
2021 ◽  
Vol 11 (11) ◽  
pp. 1263
Author(s):  
Chun-Yen Hsieh ◽  
Yi-Hao Huang ◽  
Hui-Hsuan Yeh ◽  
Pei-Yu Hong ◽  
Che-Jen Hsiao ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Cinnamic Acid ◽  
Phenylalanine Ammonia Lyase ◽  
Coumaric Acid ◽  
Wild Type ◽  
Km Value ◽  
Optimum Reaction ◽  
Bona Fide ◽  
Specific Activities ◽  
Bambusa Oldhamii

Phenylalanine ammonia-lyase (PAL) links the plant primary and secondary metabolisms, and its product, trans-cinnamic acid, is derived into thousands of diverse phenylpropanoids. Bambusa oldhamii BoPAL4 has broad substrate specificity using L-phenylalanine, L-tyrosine, and L-3,4-dihydroxy phenylalanine (L-DOPA) as substrates to yield trans-cinnamic acid, p-coumaric acid, and caffeic acid, respectively. The optimum reaction pH of BoPAL4 for three substrates was measured at 9.0, 8.5, and 9.0, respectively. The optimum reaction temperatures of BoPAL4 for three substrates were obtained at 50, 60, and 40 °C, respectively. The Km values of BoPAL4 for three substrates were 2084, 98, and 956 μM, respectively. The kcat values of BoPAL4 for three substrates were 1.44, 0.18, and 0.06 σ-1, respectively. The major substrate specificity site mutant, BoPAL4-H123F, showed better affinity toward L-phenylalanine by decreasing its Km value to 640 μM and increasing its kcat value to 1.87 s-1. In comparison to wild-type BoPAL4, the specific activities of BoPAL4-H123F using L-tyrosine and L-DOPA as substrates retained 5.4% and 17.8% residual activities. Therefore, L-phenylalanine, L-tyrosine, and L-DOPA are bona fide substrates for BoPAL4.

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
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