Enzymes
UniProtKB help_outline | 3 proteins |
Enzyme class help_outline |
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Name help_outline
an (E)-1-(glutathione-S-yl)-ω-(methylsulfanyl)alkylhydroximate
Identifier
CHEBI:136061
Charge
-1
Formula
(CH2)n.C14H23N4O7S2
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Involved in 3 reaction(s)
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Form(s) in this reaction:
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Identifier: RHEA-COMP:13138Polymer name: an S-[(1E)-1-(hydroxyimino)-ω-(methylsulfanyl)alkyl]-L-glutathionePolymerization index help_outline nFormula C14H23N4O7S2(CH2)nCharge (-1)(0)nMol File for the polymer
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- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Name help_outline
an S-[(1E)-1-(hydroxyimino)-ω-(methylsulfanyl)alkyl]-L-cysteinylglycine
Identifier
CHEBI:136825
Charge
0
Formula
(CH2)n.C9H17N3O4S2
Search links
Involved in 1 reaction(s)
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Form(s) in this reaction:
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Identifier: RHEA-COMP:13355Polymer name: an S-[(1E)-1-(hydroxyimino)-ω-(methylsulfanyl)alkyl]-L-cysteinylglycinePolymerization index help_outline nFormula C9H17N3O4S2(CH2)nCharge (0)(0)nMol File for the polymer
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- Name help_outline L-glutamate Identifier CHEBI:29985 (CAS: 11070-68-1) help_outline Charge -1 Formula C5H8NO4 InChIKeyhelp_outline WHUUTDBJXJRKMK-VKHMYHEASA-M SMILEShelp_outline [NH3+][C@@H](CCC([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 244 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:52756 | RHEA:52757 | RHEA:52758 | RHEA:52759 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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More general form(s) of this reaction
Publications
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Cytosolic gamma-glutamyl peptidases process glutathione conjugates in the biosynthesis of glucosinolates and camalexin in Arabidopsis.
Geu-Flores F., Moeldrup M.E., Boettcher C., Olsen C.E., Scheel D., Halkier B.A.
The defense-related plant metabolites known as glucosinolates play important roles in agriculture, ecology, and human health. Despite an advanced biochemical understanding of the glucosinolate pathway, the source of the reduced sulfur atom in the core glucosinolate structure remains unknown. Recen ... >> More
The defense-related plant metabolites known as glucosinolates play important roles in agriculture, ecology, and human health. Despite an advanced biochemical understanding of the glucosinolate pathway, the source of the reduced sulfur atom in the core glucosinolate structure remains unknown. Recent evidence has pointed toward GSH, which would require further involvement of a GSH conjugate processing enzyme. In this article, we show that an Arabidopsis thaliana mutant impaired in the production of the γ-glutamyl peptidases GGP1 and GGP3 has altered glucosinolate levels and accumulates up to 10 related GSH conjugates. We also show that the double mutant is impaired in the production of camalexin and accumulates high amounts of the camalexin intermediate GS-IAN upon induction. In addition, we demonstrate that the cellular and subcellular localization of GGP1 and GGP3 matches that of known glucosinolate and camalexin enzymes. Finally, we show that the purified recombinant GGPs can metabolize at least nine of the 10 glucosinolate-related GSH conjugates as well as GS-IAN. Our results demonstrate that GSH is the sulfur donor in the biosynthesis of glucosinolates and establish an in vivo function for the only known cytosolic plant γ-glutamyl peptidases, namely, the processing of GSH conjugates in the glucosinolate and camalexin pathways. << Less
Plant Cell 23:2456-2469(2011) [PubMed] [EuropePMC]
This publication is cited by 12 other entries.