Enzymes
UniProtKB help_outline | 3 proteins |
Reaction participants Show >> << Hide
- Name help_outline (Z)-4-methylsulfanylbutyl-N-(sulfonatooxy)methanimidothioate Identifier CHEBI:183222 Charge -1 Formula C6H12NO4S3 InChIKeyhelp_outline ASMOKNJFABYERB-UHFFFAOYSA-M SMILEShelp_outline [S-]/C(=[NH+]\OS([O-])(=O)=O)/CCCCSC 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 5-(methylsulfanyl)pentanenitrile Identifier CHEBI:183223 Charge 0 Formula C6H11NS InChIKeyhelp_outline XPUDGEZWSNPCMM-UHFFFAOYSA-N SMILEShelp_outline C(CCCCSC)#N 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline sulfate Identifier CHEBI:16189 (Beilstein: 3648446; CAS: 14808-79-8) help_outline Charge -2 Formula O4S InChIKeyhelp_outline QAOWNCQODCNURD-UHFFFAOYSA-L SMILEShelp_outline [O-]S([O-])(=O)=O 2D coordinates Mol file for the small molecule Search links Involved in 91 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline sulfur Identifier CHEBI:26833 (CAS: 7704-34-9) help_outline Charge 0 Formula S InChIKeyhelp_outline NINIDFKCEFEMDL-UHFFFAOYSA-N SMILEShelp_outline [S] 2D coordinates Mol file for the small molecule Search links Involved in 16 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:69328 | RHEA:69329 | RHEA:69330 | RHEA:69331 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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MetaCyc help_outline |
Related reactions help_outline
More general form(s) of this reaction
Publications
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The Arabidopsis epithiospecifier protein promotes the hydrolysis of glucosinolates to nitriles and influences Trichoplusia ni herbivory.
Lambrix V., Reichelt M., Mitchell-Olds T., Kliebenstein D.J., Gershenzon J.
Glucosinolates are anionic thioglucosides that have become one of the most frequently studied groups of defensive metabolites in plants. When tissue damage occurs, the thioglucoside linkage is hydrolyzed by enzymes known as myrosinases, resulting in the formation of a variety of products that are ... >> More
Glucosinolates are anionic thioglucosides that have become one of the most frequently studied groups of defensive metabolites in plants. When tissue damage occurs, the thioglucoside linkage is hydrolyzed by enzymes known as myrosinases, resulting in the formation of a variety of products that are active against herbivores and pathogens. In an effort to learn more about the molecular genetic and biochemical regulation of glucosinolate hydrolysis product formation, we analyzed leaf samples of 122 Arabidopsis ecotypes. A distinct polymorphism was observed with all ecotypes producing primarily isothiocyanates or primarily nitriles. The ecotypes Columbia (Col) and Landsberg erecta (Ler) differed in their hydrolysis products; therefore, the Col x Ler recombinant inbred lines were used for mapping the genes controlling this polymorphism. The major quantitative trait locus (QTL) affecting nitrile versus isothiocyanate formation was found very close to a gene encoding a homolog of a Brassica napus epithiospecifier protein (ESP), which causes the formation of epithionitriles instead of isothiocyanates during glucosinolate hydrolysis in the seeds of certain Brassicaceae. The heterologously expressed Arabidopsis ESP was able to convert glucosinolates both to epithionitriles and to simple nitriles in the presence of myrosinase, and thus it was more versatile than previously described ESPs. The role of ESP in plant defense is uncertain, because the generalist herbivore Trichoplusia ni (the cabbage looper) was found to feed more readily on nitrile-producing than on isothiocyanate-producing Arabidopsis. However, isothiocyanates are frequently used as recognition cues by specialist herbivores, and so the formation of nitriles instead of isothiocyanates may allow Arabidopsis to be less apparent to specialists. << Less
Plant Cell 13:2793-2807(2001) [PubMed] [EuropePMC]
This publication is cited by 19 other entries.
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Characterisation of recombinant epithiospecifier protein and its over-expression in Arabidopsis thaliana.
de Torres-Zabala M., Grant M., Bones A.M., Bennett R., Lim Y.S., Kissen R., Rossiter J.T.
Epithiospecifier protein (ESP) is a protein that catalyses formation of epithionitriles during glucosinolate hydrolysis. In vitro assays with a recombinant ESP showed that the formation of epithionitriles from alkenylglucosinolates is ESP and ferrous ion dependent. Nitrile formation in vitro howev ... >> More
Epithiospecifier protein (ESP) is a protein that catalyses formation of epithionitriles during glucosinolate hydrolysis. In vitro assays with a recombinant ESP showed that the formation of epithionitriles from alkenylglucosinolates is ESP and ferrous ion dependent. Nitrile formation in vitro however does not require ESP but only the presence of Fe(II) and myrosinase. Ectopic expression of ESP in Arabidopsis thaliana Col-5 under control of the strong viral CaMV 35S promoter altered the glucosinolate product profile from isothiocyanates towards the corresponding nitriles. << Less
Phytochemistry 66:859-867(2005) [PubMed] [EuropePMC]
This publication is cited by 7 other entries.