Asset Details
Do you wish to reserve the book?
CYP79D enzymes contribute to jasmonic acid-induced formation of aldoximes and other nitrogenous volatiles in two Erythroxylum species
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
CYP79D enzymes contribute to jasmonic acid-induced formation of aldoximes and other nitrogenous volatiles in two Erythroxylum species
Do you wish to request the book?
CYP79D enzymes contribute to jasmonic acid-induced formation of aldoximes and other nitrogenous volatiles in two Erythroxylum species
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
CYP79D enzymes contribute to jasmonic acid-induced formation of aldoximes and other nitrogenous volatiles in two Erythroxylum species
2016
Overview
Background
Amino acid-derived aldoximes and nitriles play important roles in plant defence. They are well-known as precursors for constitutive defence compounds such as cyanogenic glucosides and glucosinolates, but are also released as volatiles after insect feeding. Cytochrome P450 monooxygenases (CYP) of the CYP79 family catalyze the formation of aldoximes from the corresponding amino acids. However, the majority of CYP79s characterized so far are involved in cyanogenic glucoside or glucosinolate biosynthesis and only a few have been reported to be responsible for nitrogenous volatile production.
Results
In this study we analysed and compared the jasmonic acid-induced volatile blends of two
Erythroxylum
species, the cultivated South American crop species
E. coca
and the African wild species
E. fischeri
. Both species produced different nitrogenous compounds including aliphatic aldoximes and an aromatic nitrile. Four isolated
CYP79
genes (two from each species) were heterologously expressed in yeast and biochemically characterized. CYP79D62 from
E. coca
and CYP79D61 and CYP79D60 from
E. fischeri
showed broad substrate specificity
in vitro
and converted L-phenylalanine, L-isoleucine, L-leucine, L-tryptophan, and L-tyrosine into the respective aldoximes. In contrast, recombinant CYP79D63 from
E. coca
exclusively accepted L-tryptophan as substrate. Quantitative real-time PCR revealed that
CYP79D60
,
CYP79D61
, and
CYP79D62
were significantly upregulated in jasmonic acid-treated
Erythroxylum
leaves.
Conclusions
The kinetic parameters of the enzymes expressed
in vitro
coupled with the expression patterns of the corresponding genes and the accumulation and emission of (
E/Z
)-phenylacetaldoxime, (
E/Z
)-indole-3-acetaldoxime, (
E/Z
)-3-methylbutyraldoxime, and (
E
/
Z
)-2-methylbutyraldoxime in jasmonic acid-treated leaves suggest that CYP79D60, CYP79D61, and CYP79D62 accept L-phenylalanine, L-leucine, L-isoleucine, and L-tryptophan as substrates
in vivo
and contribute to the production of volatile and semi-volatile nitrogenous defence compounds in
E. coca
and
E. fischeri
.
Publisher
BioMed Central,BioMed Central Ltd,Springer Nature B.V
Subject
/ Biomedical and Life Sciences
/ Coca
/ crops
/ Cytochrome P-450 Enzyme System - chemistry
/ Cytochrome P-450 Enzyme System - genetics
/ Cytochrome P-450 Enzyme System - metabolism
/ enzymes
/ genes
/ insects
/ Leaves
/ nitriles
/ Nitrogen Compounds - metabolism
/ quantitative polymerase chain reaction
/ Real-Time Polymerase Chain Reaction
/ tyrosine
/ Volatile Organic Compounds - metabolism
/ Yeasts
