scholarly journals Cover Feature: Probing the Substrate Promiscuity of Isopentenyl Phosphate Kinase as a Platform for Hemiterpene Analogue Production (ChemBioChem 17/2019)

ChemBioChem ◽  
2019 ◽  
Vol 20 (17) ◽  
pp. 2162-2162
Author(s):  
Sean Lund ◽  
Taylor Courtney ◽  
Gavin J. Williams
Keyword(s):  
Substrate Promiscuity ◽  
Isopentenyl Phosphate

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>

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

ChemBioChem ◽  
2019 ◽  
Vol 20 (17) ◽  
pp. 2217-2221 ◽  
Author(s):  
Sean Lund ◽  
Taylor Courtney ◽  
Gavin J. Williams
Keyword(s):  
Substrate Promiscuity ◽  
Isopentenyl Phosphate

scholarly journals Molecular Basis for the Substrate Promiscuity of Isopentenyl Phosphate Kinase from Candidatus methanomethylophilus alvus

2021 ◽  
Author(s):  
Bryce P. Johnson ◽  
Vikas Kumar ◽  
Erin M. Scull ◽  
Leonard M. Thomas ◽  
Christina R. Bourne ◽  
...  
Keyword(s):  
Molecular Basis ◽  
Substrate Promiscuity ◽  
Isopentenyl Phosphate

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>

scholarly journals Structural Insights into the Substrate Promiscuity of a Laboratory-Evolved Peroxygenase

2018 ◽  
Vol 13 (12) ◽  
pp. 3259-3268 ◽  
Author(s):  
Mercedes Ramirez-Escudero ◽  
Patricia Molina-Espeja ◽  
Patricia Gomez de Santos ◽  
Martin Hofrichter ◽  
Julia Sanz-Aparicio ◽  
...  
Keyword(s):  
Substrate Promiscuity ◽  
Structural Insights

scholarly journals Extreme Substrate Promiscuity of theNeisseriaOligosaccharyl Transferase Involved in ProteinO-Glycosylation

2008 ◽  
Vol 283 (50) ◽  
pp. 34596-34604 ◽  
Author(s):  
Amirreza Faridmoayer ◽  
Messele A. Fentabil ◽  
M. Florencia Haurat ◽  
Wen Yi ◽  
Robert Woodward ◽  
...  
Keyword(s):  
Substrate Promiscuity

scholarly journals Functional Characterization and Substrate Promiscuity of UGT71 Glycosyltransferases from Strawberry (Fragaria × ananassa)

2015 ◽  
Vol 56 (12) ◽  
pp. 2478-2493 ◽  
Author(s):  
Chuankui Song ◽  
Le Gu ◽  
Jingyi Liu ◽  
Shuai Zhao ◽  
Xiaotong Hong ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Fragaria Ananassa ◽  
Substrate Promiscuity
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