Biochemical Characterization of an Arginine 2, 3‐Aminomutase with Dual Substrate Specificity

2020 ◽  
Vol 38 (9) ◽  
pp. 959-962 ◽  
Author(s):  
Junfeng Zhao ◽  
Wenjuan Ji ◽  
Xinjian Ji ◽  
Qi Zhang
Keyword(s):  
Substrate Specificity ◽  
Biochemical Characterization ◽  
Dual Substrate Specificity ◽  
Dual Substrate

scholarly journals Functional and structural characterization of a novel mannosyl-3-phosphoglycerate synthase from Rubrobacter xylanophilus reveals its dual substrate specificity

2010 ◽  
Vol 79 (1) ◽  
pp. 76-93 ◽  
Author(s):  
Nuno Empadinhas ◽  
Pedro José Barbosa Pereira ◽  
Luciana Albuquerque ◽  
Joana Costa ◽  
Bebiana Sá-Moura ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Structural Characterization ◽  
Dual Substrate Specificity ◽  
Dual Substrate

scholarly journals Biochemical Characterization of the DNA Substrate Specificity of Werner Syndrome Helicase

2002 ◽  
Vol 277 (26) ◽  
pp. 23236-23245 ◽  
Author(s):  
Robert M. Brosh ◽  
Juwaria Waheed ◽  
Joshua A. Sommers
Keyword(s):  
Substrate Specificity ◽  
Biochemical Characterization ◽  
Werner Syndrome ◽  
Dna Substrate

Biochemical characterization of two chitinases from Bacillus cereus sensu lato B25 with antifungal activity against Fusarium verticillioides P03

2020 ◽  
Author(s):  
Estefanía Morales-Ruiz ◽  
Ricardo Priego-Rivera ◽  
Alejandro Miguel Figueroa-López ◽  
Jesús Eduardo Cazares-Álvarez ◽  
Ignacio E Maldonado-Mendoza
Keyword(s):  
Bacillus Cereus ◽  
Biochemical Characterization ◽  
Fusarium Verticillioides ◽  
Expression System ◽  
Phytopathogenic Fungi ◽  
Fungal Cell ◽  
Synthetic Pesticides ◽  
Bacillus Cereus Sensu Lato ◽  
Dual Substrate

Abstract Bacterial chitinases are a subject of intense scientific research due to their biotechnological applications, particularly their use as biological pesticides against phytopathogenic fungi as a green alternative to avoid the use of synthetic pesticides. Bacillus cereus sensu lato B25 is a rhizospheric bacterium that is a proven antagonist of Fusarium verticillioides, a major fungal pathogen of maize. This bacterium produces two chitinases that degrade the fungal cell wall and inhibit its growth. In this work, we used a heterologous expression system to purify both enzymes to investigate their biochemical traits in terms of Km, Vmax, optimal pH and temperature. ChiA and ChiB work as exochitinases, but ChiB exhibited a dual substrate activity and it is also an endochitinase. In this work, the direct addition of these chitinases inhibited fungal conidial germination and therefore they may play a major role in the antagonism against F. verticillioides.

scholarly journals Origin and evolution of transporter substrate specificity within the NPF family

eLife ◽  
2017 ◽  
Vol 6 ◽  
Author(s):  
Morten Egevang Jørgensen ◽  
Deyang Xu ◽  
Christoph Crocoll ◽  
Heidi Asschenfeldt Ernst ◽  
David Ramírez ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Biochemical Characterization ◽  
Biosynthetic Pathways ◽  
Cyanogenic Glucosides ◽  
Evolutionary Path ◽  
Substrate Specificities ◽  
Origin And Evolution ◽  
Glucosinolate Biosynthesis ◽  
Phylogenetic Lineage

Despite vast diversity in metabolites and the matching substrate specificity of their transporters, little is known about how evolution of transporter substrate specificities is linked to emergence of substrates via evolution of biosynthetic pathways. Transporter specificity towards the recently evolved glucosinolates characteristic of Brassicales is shown to evolve prior to emergence of glucosinolate biosynthesis. Furthermore, we show that glucosinolate transporters belonging to the ubiquitous NRT1/PTR FAMILY (NPF) likely evolved from transporters of the ancestral cyanogenic glucosides found across more than 2500 species outside of the Brassicales. Biochemical characterization of orthologs along the phylogenetic lineage from cassava to A. thaliana, suggests that alterations in the electrogenicity of the transporters accompanied changes in substrate specificity. Linking the evolutionary path of transporter substrate specificities to that of the biosynthetic pathways, exemplify how transporter substrate specificities originate and evolve as new biosynthesis pathways emerge.

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