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  Glucosinolate hydrolysis in Lepidium sativum - identification of the thiocyanate-forming protein

Burow, M., Bergner, A., Gershenzon, J., & Wittstock, U. (2007). Glucosinolate hydrolysis in Lepidium sativum - identification of the thiocyanate-forming protein. Plant Molecular Biology, 63(1), 49-61. doi:10.1007/s11103-006-9071-5.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0012-A4E4-3 Version Permalink: https://hdl.handle.net/21.11116/0000-0009-360D-D
Genre: Journal Article

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 Creators:
Burow, M.1, 2, Author           
Bergner, A., Author
Gershenzon, J.1, Author           
Wittstock, U.1, Author           
Affiliations:
1Department of Biochemistry, MPI for Chemical Ecology, Max Planck Society, ou_421893              
2IMPRS on Ecological Interactions, MPI for Chemical Ecology, Max Planck Society, Jena, DE, ou_421900              

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Free keywords: Epithionitrile Epithiospecifier protein Glucosinolate hydrolysis Lepidium sativum Myrosinase-binding protein Organic thiocyanate Rape brassica-napus Chromatography-mass-spectrometry Thlaspi-arvense l Epithiospecifier protein Arabidopsis-thaliana Benzylglucosinolate degradation Thioglucoside glucohydrolase Liquid-chromatography Myrosinase system Plants Plant Sciences in Current Contents(R)/Agricultural, Biology & Environmental Sciences Animal & Plant Sciences in Current Contents(R)/Life Sciences
 Abstract: Glucosinolates are a class of thioglycosides found predominantly in plants of the order Brassicales whose function in anti-herbivore defense has been attributed to the products formed by myrosinase-catalyzed hydrolysis upon plant tissue damage. The most

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 Dates: 2007
 Publication Status: Issued
 Pages: -
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 Identifiers: Other: GER203
DOI: 10.1007/s11103-006-9071-5
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Title: Plant Molecular Biology
  Other : Plant Mol. Biol.
Source Genre: Journal
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Publ. Info: The Hague : Martinus Nijhoff/Dr. W. Junk
Pages: - Volume / Issue: 63 (1) Sequence Number: - Start / End Page: 49 - 61 Identifier: ISSN: 0167-4412
CoNE: https://pure.mpg.de/cone/journals/resource/954925482643