Quantification of Plant Resistance to Isoprenoid Biosynthesis Inhibitors

2014 ◽  
pp. 273-283 ◽  
Author(s):  
Catalina Perelló ◽  
Manuel Rodríguez-Concepción ◽  
Pablo Pulido
Keyword(s):  
Plant Resistance ◽  
Isoprenoid Biosynthesis ◽  
Biosynthesis Inhibitors

Synthesis and preliminary anticancer evaluation of new triazole bisphosphonate-based isoprenoid biosynthesis inhibitors

2021 ◽  
Vol 214 ◽  
pp. 113241
Author(s):  
Thibaut Legigan ◽  
Evelyne Migianu-Griffoni ◽  
Mohamed Abdenour Redouane ◽  
Aurélie Descamps ◽  
Julia Deschamp ◽  
...  
Keyword(s):  
Isoprenoid Biosynthesis ◽  
Biosynthesis Inhibitors

scholarly journals Isoprenoid Biosynthesis Inhibitors Targeting Bacterial Cell Growth

ChemMedChem ◽  
2016 ◽  
Vol 11 (19) ◽  
pp. 2205-2215 ◽  
Author(s):  
Janish Desai ◽  
Yang Wang ◽  
Ke Wang ◽  
Satish R. Malwal ◽  
Eric Oldfield
Keyword(s):  
Cell Growth ◽  
Bacterial Cell ◽  
Isoprenoid Biosynthesis ◽  
Biosynthesis Inhibitors

Probing the Substrate Promiscuity of Isopentenyl Phosphate Kinase as a Platform for Hemiterpene Analogue Production

2019 ◽  
Author(s):  
Sean Lund ◽  
Taylor Courtney ◽  
Gavin Williams
Keyword(s):  
Synthetic Biology ◽  
Building Blocks ◽  
Isoprenoid Biosynthesis ◽  
Thermoplasma Acidophilum ◽  
Substrate Promiscuity ◽  
Enzymatic Pathways ◽  
First Time ◽  
Rate Limiting ◽  
Alcohol Dependent ◽  
Isopentenyl Phosphate

Isoprenoids are a large class of natural products with wide-ranging applications. Synthetic biology approaches to the manufacture of isoprenoids and their new-to-nature derivatives are limited due to the provision in Nature of just two hemiterpene building blocks for isoprenoid biosynthesis. To address this limitation, artificial chemo-enzymatic pathways such as the alcohol-dependent hemiterpene pathway (ADH) serve to leverage consecutive kinases to convert exogenous alcohols to pyrophosphates that could be coupled to downstream isoprenoid biosynthesis. To be successful, each kinase in this pathway should be permissive of a broad range of substrates. For the first time, we have probed the promiscuity of the second enzyme in the ADH pathway, isopentenyl phosphate kinase from Thermoplasma acidophilum, towards a broad range of acceptor monophosphates. Subsequently, we evaluate the suitability of this enzyme to provide non-natural pyrophosphates and provide a critical first step in characterizing the rate limiting steps in the artificial ADH pathway.<br>

Decreased sensitivity of cucumber powdery mildew (Sphaerotheca fuliginea) to ergosterol biosynthesis inhibitors.

1988 ◽  
Vol 54 (5) ◽  
pp. 629-632 ◽  
Author(s):  
Norio OHTSUKA ◽  
Kazuhiro SOU ◽  
Tetsuo AMANO ◽  
Masahiro OJIMA ◽  
Yasuhiko NAKAZAWA ◽  
...  
Keyword(s):  
Powdery Mildew ◽  
Ergosterol Biosynthesis ◽  
Sphaerotheca Fuliginea ◽  
Cucumber Powdery Mildew ◽  
Ergosterol Biosynthesis Inhibitors ◽  
Biosynthesis Inhibitors
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