The role of cytochrome P450 enzymes in the biosynthesis of camalexin

2006 ◽  
Vol 34 (6) ◽  
pp. 1206-1208 ◽  
Author(s):  
E. Glawischnig

The biosynthesis of camalexin, the main phytoalexin of the model plant Arabidopsis thaliana, involves at least two CYP (cytochrome P450) steps. It is synthesized from tryptophan via indole-3-acetaldoxime in a reaction catalysed by CYP79B2 and CYP79B3. Based on the pad3 mutant phenotype, CYP71B15 (PAD3) had also been suggested as a camalexin biosynthetic gene. CYP71B15 catalyses the final step in camalexin biosynthesis, as recombinant CYP71B15 and microsomes from Arabidopsis leaves expressing functional PAD3 converted dihydrocamalexic acid into camalexin. The biosynthetic pathway is co-ordinately induced, strictly localized to the site of pathogen infection. This provides a model system to study the regulation of CYP enzymes involved in phytoalexin biosynthesis.

2017 ◽  
Vol 22 (4) ◽  
pp. 382-392 ◽  
Author(s):  
Vibhav Gautam ◽  
Archita Singh ◽  
Swati Verma ◽  
Ashutosh Kumar ◽  
Pramod Kumar ◽  
...  

2017 ◽  
Vol 51 (20) ◽  
pp. 12007-12015 ◽  
Author(s):  
Zunwei Chen ◽  
Jia Wang ◽  
Hui Chen ◽  
Yuezhong Wen ◽  
Weiping Liu

2002 ◽  
Vol 30 (2) ◽  
pp. 301-306 ◽  
Author(s):  
D. Bowles

Glycosyltransferases transfer sugars from NDP-sugar donors to acceptors. The multigene family of transferases described in this paper typically transfer glucose from UDP-glucose to low-molecular-mass acceptors in the cytosol of plant cells. There are 107 sequences in the genome of Arabidopsis thaliana that contain a consensus, suggesting they belong to this Group 1 multigene family. The family has been analysed phylogenetically, and a functional genomics approach has been applied to explore the relatedness of sequence similarity to catalytic specificity and stereoselectivity. Enzymes belonging to this class of transferases glycosylate a vast array of acceptors, including natural products such as secondary metabolites and hormones, as well as xenobiotics absorbed by the plant, such as herbicides and pesticides. Conjugation to glucose potentially changes the activity of the acceptor molecule and invariably changes its location within the plant cell. Using the genomics approach described, a platform of knowledge has been constructed that will enable an understanding to be gained on the role of these enzymes in cellular homoeostasis, as well as their activity in biotransformations in vitro that require strict regioselectivity of glycosylation.


2008 ◽  
Vol 36 (8) ◽  
pp. 1637-1649 ◽  
Author(s):  
Robin E. Pearce ◽  
Wei Lu ◽  
YongQiang Wang ◽  
Jack P. Uetrecht ◽  
Maria Almira Correia ◽  
...  

2021 ◽  
Vol 189 ◽  
pp. 112822
Author(s):  
Reinmar Eggers ◽  
Alexandra Jammer ◽  
Shalinee Jha ◽  
Bianca Kerschbaumer ◽  
Majd Lahham ◽  
...  

2020 ◽  
Vol 21 (15) ◽  
pp. 5371 ◽  
Author(s):  
Patrick Schall ◽  
Lucas Marutschke ◽  
Bernhard Grimm

Flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) are essential cofactors for enzymes, which catalyze a broad spectrum of vital reactions. This paper intends to compile all potential FAD/FMN-binding proteins encoded by the genome of Arabidopsis thaliana. Several computational approaches were applied to group the entire flavoproteome according to (i) different catalytic reactions in enzyme classes, (ii) the localization in subcellular compartments, (iii) different protein families and subclasses, and (iv) their classification to structural properties. Subsequently, the physiological significance of several of the larger flavoprotein families was highlighted. It is conclusive that plants, such as Arabidopsis thaliana, use many flavoenzymes for plant-specific and pivotal metabolic activities during development and for signal transduction pathways in response to biotic and abiotic stress. Thereby, often two up to several homologous genes are found encoding proteins with high protein similarity. It is proposed that these gene families for flavoproteins reflect presumably their need for differential transcriptional control or the expression of similar proteins with modified flavin-binding properties or catalytic activities.


Sign in / Sign up

Export Citation Format

Share Document