scholarly journals The Role of Cytochrome P450 Monooxygenases in Plant-Insect Interactions

1996 ◽  
Vol 112 (4) ◽  
pp. 1411-1419 ◽  
Author(s):  
M. A. Schuler
Keyword(s):  
Cytochrome P450 ◽  
Cytochrome P450 Monooxygenases ◽  
Plant Insect Interactions ◽  
P450 Monooxygenases ◽  
Insect Interactions

scholarly journals The Role of Cytochrome P450s in Insect Toxicology and Resistance

2021 ◽  
Vol 67 (1) ◽  
Author(s):  
Ralf Nauen ◽  
Chris Bass ◽  
René Feyereisen ◽  
John Vontas
Keyword(s):  
Cytochrome P450 ◽  
Insecticide Resistance ◽  
Insect Pests ◽  
Cytochrome P450s ◽  
Cytochrome P450 Monooxygenases ◽  
Annual Review ◽  
Publication Date ◽  
Beneficial Insects ◽  
P450 Monooxygenases

Insect cytochrome P450 monooxygenases (P450s) perform a variety of important physiological functions, but it is their role in the detoxification of xenobiotics, such as natural and synthetic insecticides, that is the topic of this review. Recent advances in insect genomics and postgenomic functional approaches have provided an unprecedented opportunity to understand the evolution of insect P450s and their role in insect toxicology. These approaches have also been harnessed to provide new insights into the genomic alterations that lead to insecticide resistance, the mechanisms by which P450s are regulated, and the functional determinants of P450-mediated insecticide resistance. In parallel, an emerging body of work on the role of P450s in defining the sensitivity of beneficial insects to insecticides has been developed. The knowledge gained from these studies has applications for the management of P450-mediated resistance in insect pests and can be leveraged to safeguard the health of important beneficial insects. Expected final online publication date for the Annual Review of Entomology, Volume 67 is January 2022. Please see http://www.annualreviews.org/page/journal/pubdates for revised estimates.

scholarly journals The central role of mosquito cytochrome P450 CYP6Zs in insecticide detoxification revealed by functional expression and structural modelling

2013 ◽  
Vol 455 (1) ◽  
pp. 75-85 ◽  
Author(s):  
Alexia Chandor-Proust ◽  
Jaclyn Bibby ◽  
Myriam Régent-Kloeckner ◽  
Jessica Roux ◽  
Emilie Guittard-Crilat ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
In Silico ◽  
Functional Expression ◽  
Cytochrome P450 Monooxygenases ◽  
Structural Modelling ◽  
P450 Monooxygenases ◽  
In Silico Modelling

The key role of mosquito cytochrome P450 monooxygenases from the CYP6Z subfamily in the resistance of mosquitoes to insecticides was revealed. By using functional expression and in silico modelling, the capacity of CYP6Zs to degrade insecticide metabolites produced by esterase-mediated hydrolysis was demonstrated.

The role of cytochrome P450 monooxygenases in microbial fatty acid metabolism

FEBS Journal ◽  
2010 ◽  
Vol 278 (2) ◽  
pp. 206-221 ◽  
Author(s):  
Inge N. A. Van Bogaert ◽  
Sara Groeneboer ◽  
Karen Saerens ◽  
Wim Soetaert
Keyword(s):  
Cytochrome P450 ◽  
Fatty Acid ◽  
Fatty Acid Metabolism ◽  
Acid Metabolism ◽  
Cytochrome P450 Monooxygenases ◽  
P450 Monooxygenases ◽  
Microbial Fatty Acid

Characterization of cytochrome P450-monooxygenases of Chinese hamsters with respect to aflatoxin B1 activation

Toxicology ◽  
1994 ◽  
Vol 93 (2-3) ◽  
pp. 165-173 ◽  
Author(s):  
Morio Fukuhara ◽  
Eric Antignac ◽  
Naomi Fukusen ◽  
Kazue Kato ◽  
Masanobu Kimura
Keyword(s):  
Cytochrome P450 ◽  
Aflatoxin B1 ◽  
Cytochrome P450 Monooxygenases ◽  
P450 Monooxygenases ◽  
Chinese Hamsters

scholarly journals Specificity and mechanism of carbohydrate demethylation by cytochrome P450 monooxygenases

2018 ◽  
Vol 475 (23) ◽  
pp. 3875-3886 ◽  
Author(s):  
Craig S. Robb ◽  
Lukas Reisky ◽  
Uwe T. Bornscheuer ◽  
Jan-Hendrik Hehemann
Keyword(s):  
Cytochrome P450 ◽  
Active Site ◽  
Substrate Recognition ◽  
High Energy ◽  
Cytochrome P450 Monooxygenases ◽  
P450 Monooxygenases ◽  
High Energy Barrier ◽  
Molecular Determinants ◽  
Cytochrome P450 Family ◽  
Carbohydrate Ligand

Degradation of carbohydrates by bacteria represents a key step in energy metabolism that can be inhibited by methylated sugars. Removal of methyl groups, which is critical for further processing, poses a biocatalytic challenge because enzymes need to overcome a high energy barrier. Our structural and computational analysis revealed how a member of the cytochrome P450 family evolved to oxidize a carbohydrate ligand. Using structural biology, we ascertained the molecular determinants of substrate specificity and revealed a highly specialized active site complementary to the substrate chemistry. Invariance of the residues involved in substrate recognition across the subfamily suggests that they are critical for enzyme function and when mutated, the enzyme lost substrate recognition. The structure of a carbohydrate-active P450 adds mechanistic insight into monooxygenase action on a methylated monosaccharide and reveals the broad conservation of the active site machinery across the subfamily.

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