The versatility of the fungal cytochrome P450 monooxygenase system is instrumental in xenobiotic detoxification
Lah, Ljerka (Author), Podobnik, Barbara (Author), Novak, Metka (Author), Korošec, Branka (Author), Berne, Sabina (Author), Vogelsang, Matjaž (Author), Kraševec, Nada (Author), Šamec, Neja (Author), Stojan, Jure (Author), Bohlmann, Joerg (Author), Komel, Radovan (Author)

URLURL - Presentation file, Visit http://onlinelibrary.wiley.com/doi/10.1111/j.1365-2958.2011.07772.x/full This link opens in a new window

Cytochromes P450 (CYPs) catalyse diverse reactions and are key enzymes in fungal primary and secondary metabolism, and xenobiotic detoxification. CYP enzymatic properties and substrate specificity determine the reaction outcome. However, CYP-mediated reactions may also be influenced by their redox partners. Filamentous fungi with numerous CYPs often possess multiple microsomal redox partners, cytochrome P450 reductases (CPRs). In the plant pathogenic ascomycete Cochliobolus lunatus we recently identified two CPR paralogues, CPR1 and CPR2. Our objective was to functionally characterize two endogenous fungal cytochrome P450 systems and elucidate the putative physiological roles of CPR1 and CPR2. We reconstituted both CPRs with CYP53A15, or benzoate 4-hydroxylase from C. lunatus, which is crucial in the detoxification of phenolic plant defence compounds. Biochemical characterization using RP-HPLC shows that both redox partners support CYP activity, but with different product specificities. When reconstituted with CPR1, CYP53A15 converts benzoic acid to 4-hydroxybenzoic acid, and 3-methoxybenzoic acid to 3-hydroxybenzoic acid. However, when the redox partner is CPR2, both substrates are converted to 3,4-dihydroxybenzoic acid. Deletion mutants and gene expression in mycelia grown on media with inhibitors indicate that CPR1 is important in primary metabolism, whereas CPR2 plays a role in xenobiotic detoxification.

Keywords:strukturna kemija, sinteza snovi, detoksikacija
Work type:Not categorized (r6)
Tipology:1.01 - Original Scientific Article
Organization:NTF - Faculty of Natural Sciences and Engineering
Number of pages:str. 1374-1389
Numbering:Vol. 85, iss. 5
ISSN on article:0950-382X
DOI:10.1111/j.1365-2958.2011.07772.x Link is opened in a new window
COBISS.SI-ID:4729882 Link is opened in a new window
Average score:(0 votes)
Your score:Voting is allowed only to logged in users.
AddThis uses cookies that require your consent. Edit consent...

Record is a part of a journal

Title:Molecular microbiology
Shortened title:Mol. microbiol.
Publisher:Blackwell Scientific
COBISS.SI-ID:27168000 This link opens in a new window

Similar documents

Similar works from RUL:
Similar works from other Slovenian collections:


Leave comment

You have to log in to leave a comment.

Comments (0)
0 - 0 / 0
There are no comments!