The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
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The gene GGP1 (At4g30530, UniProt accession Q9M0A7) encodes gamma-glutamyl peptidase 1 in Arabidopsis thaliana. The protein belongs to the peptidase C26 family and carries the EC number 3.4.19.16 (ito2022glutathionedegradationactivity pages 11-12). This identity matches the UniProt annotation and is consistently described across multiple authoritative studies. GGP1 should not be confused with CGEP (chloroplast glutamyl peptidase), which is an unrelated chloroplast stromal S9D serine peptidase also present in Arabidopsis (bhuiyan2020autocatalyticprocessingand pages 1-2, bhuiyan2020autocatalyticprocessingand pages 2-3).
GGP1 catalyzes the hydrolysis of the γ-glutamyl bond in reduced glutathione (GSH) and related glutathione conjugates. The primary reaction is: GSH + H₂O → L-glutamate + L-cysteinylglycine (ito2022glutathionedegradationactivity pages 2-3, ito2022glutathionedegradationactivity pages 1-2). This enzymatic activity directly releases glutamate without requiring ATP, making it more energy-efficient than the alternative γ-glutamyl cyclotransferase (GGCT) pathway, which produces 5-oxoproline that must subsequently be converted to glutamate in an ATP-dependent manner (ito2022glutathionedegradationactivity pages 11-12).
As a member of the C26 cysteine peptidase family (MEROPS classification), GGP1 employs a conserved catalytic triad consisting of Cys100, His192, and Glu194 (ito2022glutathionedegradationactivity pages 11-12). AlphaFold-based structural modeling has identified additional substrate-interacting residues including Gln104, Gln156, Asp157, Arg206, and Tyr212, which contribute to recognition and positioning of the γ-glutamyl, glycine, and hydrophobic portions of substrates (ito2022glutathionedegradationactivity pages 11-12).
Detailed enzyme kinetic studies using purified recombinant GGP1 revealed the following parameters for GSH hydrolysis: apparent Km = 5.0 mM, kcat = 0.33 s⁻¹, and catalytic efficiency (kcat/Km) = 66 M⁻¹ s⁻¹ (ito2022glutathionedegradationactivity pages 2-3, ito2022glutathionedegradationactivity pages 3-5). The Km value is physiologically relevant given reported cytosolic GSH concentrations in plants (ito2022glutathionedegradationactivity pages 9-11).
GGP1 exhibits notable substrate selectivity. It shows robust activity toward reduced GSH but little or no detectable activity toward oxidized glutathione (GSSG), γ-glutamylcysteine (γ-Glu-Cys), or γ-glutamylalanine (γ-Glu-Ala) (ito2022glutathionedegradationactivity pages 2-3, ito2022glutathionedegradationactivity pages 1-2). Beyond free GSH, GGP1 processes at least nine structurally diverse glucosinolate-related GSH conjugates bearing methylsulfinylalkyl, methylthioalkyl, and indol-3-ylmethyl side chains (geuflores2011cytosolicγglutamylpeptidases pages 5-7, geuflores2011cytosolicγglutamylpeptidases pages 8-10). The enzyme also accepts GS-IAN (S-[(indol-3-yl)acetonitrile]-L-glutathione), a GSH conjugate intermediate in camalexin biosynthesis (geuflores2011cytosolicγglutamylpeptidases pages 5-7, geuflores2011cytosolicγglutamylpeptidases pages 1-2).
Importantly, GGP1 shows substantially higher affinity for GSH conjugates than for free GSH. For example, the reported Km for the model glucosinolate conjugate GS-B is approximately 37–8 μM, compared to 5.0 mM for GSH (ito2022glutathionedegradationactivity pages 11-12). This differential affinity suggests that conjugate processing may take precedence when conjugates accumulate, while GSH degradation becomes more prominent under conditions when conjugate levels are low (ito2022glutathionedegradationactivity pages 12-13).
GGP1 is a cytosolic enzyme. Multiple lines of experimental evidence support this localization:
Fluorescent protein fusion studies: C-terminal GGP1-YFP fusions transiently expressed in Nicotiana benthamiana epidermal cells and mesophyll protoplasts showed cytosolic fluorescence patterns when examined by confocal laser scanning microscopy (geuflores2011cytosolicγglutamylpeptidases pages 4-5, geuflores2011cytosolicγglutamylpeptidases pages 2-4).
Biochemical fractionation: Recombinant GGP1 expressed in Escherichia coli was recovered from the soluble fraction, consistent with cytosolic rather than membrane-associated localization (ito2022glutathionedegradationactivity pages 2-3).
Functional compatibility: The cytosolic localization aligns with the known compartmentation of related pathway enzymes. The cytochrome P450 enzymes involved in glucosinolate biosynthesis have their catalytic domains facing the cytosol, and the glutathione S-transferase GSTF6, which generates GSH conjugates, is predicted to be cytosolic (geuflores2011cytosolicγglutamylpeptidases pages 8-10).
GGP1 functions inside the cell within the cytosolic compartment, where it has access to both cytosolic GSH and the GSH conjugates generated during specialized metabolite biosynthesis (ito2022glutathionedegradationactivity pages 2-3, ito2022glutathionedegradationactivity pages 1-2).
Quantitative RT-PCR expression profiling revealed that GGP1 transcripts are present in all examined organs but are particularly abundant in mature rosette leaves (ito2022glutathionedegradationactivity pages 3-5, ito2022glutathionedegradationactivity pages 9-11). Promoter-GUS reporter experiments using approximately 2 kb of the GGP1 promoter region driving GUS expression showed that GGP1 is expressed in or near vascular tissues in Arabidopsis leaves (geuflores2011cytosolicγglutamylpeptidases pages 4-5). This spatial expression pattern matches the sites where glucosinolate biosynthetic enzymes are predominantly active (ito2022glutathionedegradationactivity pages 9-11).
GGP1 plays dual roles in plant sulfur metabolism, participating in both primary and secondary metabolic pathways (ito2022glutathionedegradationactivity pages 11-12, ito2022glutathionedegradationactivity pages 1-2).
GGP1 serves as a major enzyme responsible for degrading cytosolic GSH, particularly under sulfur-sufficient or normal growth conditions (ito2022glutathionedegradationactivity pages 9-11, ito2022glutathionedegradationactivity pages 11-12). This function was definitively established through multiple experimental approaches:
Yeast complementation: Arabidopsis GGP1 rescued Saccharomyces cerevisiae dug2Δ and dug3Δ mutants, which are defective in GSH utilization, enabling growth when GSH was the sole sulfur source (ito2022glutathionedegradationactivity pages 3-5, ito2022glutathionedegradationactivity pages 2-3).
Mutant phenotypes: Independent ggp1 knockout lines consistently accumulated significantly more GSH than wild-type plants under normal growth conditions, demonstrating impaired GSH degradation (ito2022glutathionedegradationactivity pages 3-5, ito2022glutathionedegradationactivity pages 1-2). The elevated GSH was observed regardless of nutritional conditions, indicating that GGP1 constitutively contributes to GSH turnover (ito2022glutathionedegradationactivity pages 9-11).
GSH degradation by GGP1 releases glutamate, cysteine (via Cys-Gly), and glycine, supporting amino acid homeostasis and enabling sulfur reallocation within the plant (ito2022glutathionedegradationactivity pages 9-11, ito2022glutathionedegradationactivity pages 6-7). Under sulfur deficiency, the related enzyme GGCT2;1 is strongly induced and accelerates GSH degradation, supplementing or partially replacing GGP1 activity (ito2022glutathionedegradationactivity pages 11-12). However, GGP1 appears to provide the principal, constitutive route for cytosolic GSH breakdown under ordinary conditions (ito2022glutathionedegradationactivity pages 9-11).
GGP1 plays an essential role in glucosinolate biosynthesis by processing GSH conjugates formed during the pathway. Glucosinolates are sulfur-containing defense compounds characteristic of the Brassicales order that are important for plant defense against herbivores and pathogens (geuflores2011cytosolicγglutamylpeptidases pages 5-7, geuflores2011cytosolicγglutamylpeptidases pages 1-2).
The biochemical evidence for GGP1's role includes:
In vitro substrate processing: Purified recombinant GGP1 hydrolyzed nine of ten glucosinolate-related GSH conjugates detected in mutant plants, converting them to corresponding Cys-Gly conjugates (geuflores2011cytosolicγglutamylpeptidases pages 5-7, geuflores2011cytosolicγglutamylpeptidases pages 8-10).
Mutant accumulation of intermediates: The ggp1-1 ggp3-1 double mutant accumulated up to ten glucosinolate-related GSH conjugates that are normally processed, demonstrating blockage at the γ-glutamyl cleavage step (geuflores2011cytosolicγglutamylpeptidases pages 5-7, geuflores2011cytosolicγglutamylpeptidases pages 7-8).
Altered glucosinolate profiles: Loss of GGP1 and GGP3 function resulted in reduced levels of long-chain methionine-derived glucosinolates, particularly 6-methylsulfinylhexyl (6MSH), 7-methylsulfinylheptyl (7MSH), and 8-methylsulfinyloctyl (8MSO) glucosinolates (ito2022glutathionedegradationactivity pages 7-8, ito2022glutathionedegradationactivity pages 6-7). Corresponding isothiocyanate breakdown products, including sulforaphane-related compounds, were also reduced in ggp1 mutants (ito2022glutathionedegradationactivity pages 7-8).
These findings established that GSH (rather than free cysteine) serves as the sulfur donor in glucosinolate biosynthesis, with GGP1 removing the γ-glutamyl group from conjugated intermediates to enable progression toward the mature glucosinolate structure (geuflores2011cytosolicγglutamylpeptidases pages 1-2, geuflores2011cytosolicγglutamylpeptidases pages 2-4).
GGP1 also participates in the biosynthesis of camalexin, an indolic phytoalexin produced in response to pathogen challenge. The enzyme processes GS-IAN (the GSH conjugate of indole-3-acetonitrile), yielding Cys-Gly-IAN and supporting camalexin accumulation (geuflores2011cytosolicγglutamylpeptidases pages 5-7, geuflores2011cytosolicγglutamylpeptidases pages 1-2). The ggp1-1 single mutant showed reduced camalexin production, and the ggp1-1 ggp3-1 double mutant exhibited an even stronger reduction, with high accumulation of GS-IAN upon camalexin induction (geuflores2011cytosolicγglutamylpeptidases pages 8-10, geuflores2011cytosolicγglutamylpeptidases pages 7-8).
ggp1 mutants accumulated higher levels of O-acetyl-L-serine (OAS), a signaling molecule associated with sulfur starvation responses, particularly under sulfur-deficient conditions (ito2022glutathionedegradationactivity pages 7-8, ito2022glutathionedegradationactivity pages 1-2). This suggests that impaired GGP1 function affects sulfur-status perception or signaling, potentially because reduced GSH turnover limits sulfur reallocation and triggers compensatory responses (ito2022glutathionedegradationactivity pages 8-9).
The functional characterization of GGP1 is supported by multiple complementary experimental approaches:
T-DNA insertion mutants: Independent knockout lines (ggp1-1, ggp1-2) were generated and characterized, with ggp1-1 retaining only 0.7–1.0% of wild-type GGP1 transcript levels (ito2022glutathionedegradationactivity pages 3-5, geuflores2011cytosolicγglutamylpeptidases pages 2-4).
Artificial microRNA knockdown: To overcome functional redundancy with GGP3 (which is genetically linked to GGP1), researchers created a ggp1-1 ggp3-1 double mutant using amiRNA-mediated GGP3 knockdown, resulting in plants with approximately 1–4% of wild-type GGP1 and 6–30% of wild-type GGP3 transcripts (geuflores2011cytosolicγglutamylpeptidases pages 4-5).
Heterologous complementation: Expression of Arabidopsis GGP1 in yeast GSH-utilization mutants fully rescued their growth defect, demonstrating that GGP1 alone is sufficient to support GSH degradation (ito2022glutathionedegradationactivity pages 3-5, ito2022glutathionedegradationactivity pages 2-3).
Enzyme kinetics: Detailed Michaelis-Menten kinetics were determined using purified recombinant protein expressed in E. coli (ito2022glutathionedegradationactivity pages 3-5, ito2022glutathionedegradationactivity pages 2-3).
Substrate specificity profiling: A panel of γ-glutamyl compounds and GSH derivatives was tested to define the enzyme's substrate selectivity (ito2022glutathionedegradationactivity pages 2-3, geuflores2011cytosolicγglutamylpeptidases pages 5-7).
Targeted and untargeted metabolomics: Widely targeted metabolomics and specific analyses of glucosinolates, isothiocyanates, GSH, OAS, and related compounds were performed on wild-type and mutant plants under multiple nutrient conditions (ito2022glutathionedegradationactivity pages 7-8, ito2022glutathionedegradationactivity pages 6-7, ito2022glutathionedegradationactivity pages 8-9).
GSH conjugate profiling: Accumulated GSH conjugates in the double mutant were identified and quantified, with structures confirmed using synthetic standards where available (geuflores2011cytosolicγglutamylpeptidases pages 5-7, geuflores2011cytosolicγglutamylpeptidases pages 7-8).
Structural modeling: AlphaFold prediction of GGP1 structure identified the C26 peptidase fold and catalytic triad (ito2022glutathionedegradationactivity pages 11-12, ito2022glutathionedegradationactivity pages 12-13).
Substrate docking: Modeling of the glucosinolate conjugate GS-B into the predicted GGP1 active site identified key substrate-binding residues (ito2022glutathionedegradationactivity pages 11-12).
Coexpression analysis: Transcriptome-wide coexpression analyses linked GGP1 with sulfur-assimilation genes (APS1, APR1, APK1/2, APS3, SERAT2;2) and glucosinolate biosynthesis genes, supporting its role in coordinating sulfur allocation between primary and secondary metabolism (ito2022glutathionedegradationactivity pages 12-13).
| Property | Description |
|---|---|
| Basic protein information | Gene: GGP1; ordered locus: At4g30530; organism: Arabidopsis thaliana; UniProt: Q9M0A7; recommended name: γ-glutamyl peptidase 1; EC: 3.4.19.16; family: cysteine peptidase C26; annotated domains/folds: ChyE-like and class-I glutamine-amidotransferase-like/GATase. These identifiers agree with the experimentally studied cytosolic GGP1. It must not be confused with CGEP, an unrelated chloroplast S9D serine peptidase. (ito2022glutathionedegradationactivity pages 11-12) |
| Enzymatic function and catalytic mechanism | GGP1 hydrolyzes the γ-glutamyl bond of reduced glutathione: GSH + H₂O → L-glutamate + L-cysteinylglycine. It likewise removes the γ-glutamyl group from glutathione conjugates, producing corresponding Cys-Gly conjugates. As a C26 cysteine peptidase, it is predicted to use the conserved Cys100–His192–Glu194 catalytic triad. Direct glutamate production avoids the ATP-dependent conversion of 5-oxoproline required by the alternative γ-glutamyl-cyclotransferase pathway. (ito2022glutathionedegradationactivity pages 2-3, ito2022glutathionedegradationactivity pages 11-12) |
| Substrate specificity and kinetics | Purified recombinant GGP1 degraded reduced GSH with apparent Kₘ = 5.0 mM, kcat = 0.33 s⁻¹, and catalytic efficiency = 66 M⁻¹ s⁻¹. Little or no activity was detected toward oxidized glutathione, γ-glutamylcysteine, or γ-glutamylalanine. GGP1 also accepts at least nine structurally diverse glucosinolate-related GSH conjugates and the camalexin intermediate GS-IAN. Its reported affinity for the model conjugate GS-B is substantially higher than for free GSH. (ito2022glutathionedegradationactivity pages 11-12, ito2022glutathionedegradationactivity pages 3-5, ito2022glutathionedegradationactivity pages 2-3, geuflores2011cytosolicγglutamylpeptidases pages 5-7) |
| Subcellular localization | Cytosolic. C-terminal GGP1–YFP expressed transiently in Nicotiana benthamiana epidermal cells and mesophyll protoplasts produced a cytosolic fluorescence pattern. This localization is consistent with access to cytosolic GSH and the cytosol-facing steps of glucosinolate and camalexin synthesis. There is no evidence that Q9M0A7 is secreted or functions in the chloroplast, vacuole, or apoplast. (ito2022glutathionedegradationactivity pages 2-3, ito2022glutathionedegradationactivity pages 1-2, geuflores2011cytosolicγglutamylpeptidases pages 4-5) |
| Tissue and cellular expression | GGP1 transcripts occur in all examined organs but are especially abundant in mature rosette leaves. Promoter–GUS experiments showed expression associated with leaf vascular tissue, spatially matching major sites of glucosinolate-pathway activity. (ito2022glutathionedegradationactivity pages 9-11, ito2022glutathionedegradationactivity pages 3-5, geuflores2011cytosolicγglutamylpeptidases pages 4-5) |
| Primary sulfur metabolism | GGP1 is proposed to mediate a major component of basal cytosolic GSH turnover, releasing glutamate and Cys-Gly for subsequent amino-acid recovery. Its kinetic properties are compatible with cytosolic GSH concentrations. Under sulfur deficiency, induced GGCT2;1 supplements this pathway, whereas GGP1 appears particularly important under sulfur-sufficient or ordinary growth conditions. (ito2022glutathionedegradationactivity pages 9-11, ito2022glutathionedegradationactivity pages 11-12) |
| Specialized-metabolite pathways | In glucosinolate biosynthesis, GGP1 removes glutamate from pathway-specific GSH conjugates, supporting the conclusion that GSH supplies reduced sulfur and enabling progression toward thiohydroximate intermediates. In camalexin biosynthesis, it converts GS-IAN to Cys-Gly-IAN. GGP3 provides overlapping activity, explaining why strong defects are clearest when both enzymes are impaired. (geuflores2011cytosolicγglutamylpeptidases pages 5-7, geuflores2011cytosolicγglutamylpeptidases pages 1-2, geuflores2011cytosolicγglutamylpeptidases pages 2-4) |
| Key experimental evidence | Evidence includes rescue of GSH-utilization-defective yeast dug2Δ and dug3Δ mutants by Arabidopsis GGP1; direct kinetic and specificity assays with purified recombinant enzyme; GGP1–YFP localization; promoter–GUS expression mapping; metabolomics of single and combined mutants; and structural modeling that places GSH conjugates beside the conserved C26 catalytic triad and implicates Gln104, Gln156, Asp157, Arg206, and Tyr212 in substrate recognition. (ito2022glutathionedegradationactivity pages 3-5, ito2022glutathionedegradationactivity pages 11-12, ito2022glutathionedegradationactivity pages 12-13, geuflores2011cytosolicγglutamylpeptidases pages 4-5) |
| Mutant phenotypes | Independent ggp1 knockout or strong-loss lines accumulate significantly more GSH than wild type under normal and altered nutrient conditions, supporting defective degradation rather than enhanced synthesis. They also show increased O-acetyl-L-serine under sulfur deficiency and reduced levels of several glucosinolates and isothiocyanate products. Combined impairment of GGP1 and GGP3 causes accumulation of up to ten pathway-related GSH conjugates, reduced long-chain methionine-derived glucosinolates, GS-IAN accumulation, and impaired induced camalexin production. (ito2022glutathionedegradationactivity pages 7-8, ito2022glutathionedegradationactivity pages 3-5, ito2022glutathionedegradationactivity pages 1-2, geuflores2011cytosolicγglutamylpeptidases pages 7-8) |
| Functional interpretation | The best-supported annotation is a cytosolic C26 γ-glutamyl peptidase with dual roles: degradation of reduced GSH in primary sulfur metabolism and processing of specialized GSH conjugates in glucosinolate and camalexin biosynthesis. GGP3 and GGCT enzymes provide partial redundancy, so phenotypes depend on tissue, nutrient status, and substrate availability. (ito2022glutathionedegradationactivity pages 11-12, ito2022glutathionedegradationactivity pages 1-2) |
Table: Key biochemical, localization, pathway, structural, and genetic evidence for Arabidopsis thaliana GGP1 (At4g30530; UniProt Q9M0A7). The table distinguishes this cytosolic C26 cysteine peptidase from the unrelated chloroplast S9D glutamyl peptidase CGEP.
The comprehensive characterization of GGP1 reveals it as a bifunctional enzyme operating at the interface of primary and secondary sulfur metabolism in Arabidopsis. Its dual substrate specificity—accepting both free GSH and specialized GSH conjugates—enables it to balance glutathione homeostasis with the production of defensive glucosinolates and phytoalexins (ito2022glutathionedegradationactivity pages 11-12, ito2022glutathionedegradationactivity pages 1-2).
The higher affinity of GGP1 for GSH conjugates compared to free GSH (Km ~37–8 μM vs. 5.0 mM) suggests a substrate-prioritization mechanism: when glucosinolate or camalexin biosynthesis is active and conjugates accumulate, GGP1 preferentially processes these pathway intermediates; when conjugate levels are low, it contributes to basal GSH turnover (ito2022glutathionedegradationactivity pages 11-12, ito2022glutathionedegradationactivity pages 12-13). This biochemical strategy may allow plants to coordinate sulfur allocation in response to developmental and environmental cues.
The energy efficiency of the GGP-mediated pathway compared to the GGCT pathway (direct glutamate production versus ATP-dependent conversion from 5-oxoproline) may explain why GGP1 provides the predominant route for GSH degradation in mature photosynthetic tissues where energy conservation is advantageous (ito2022glutathionedegradationactivity pages 11-12). The functional redundancy with GGP3 and the nutrient-responsive induction of GGCT2;1 provide additional layers of regulation, ensuring robust GSH turnover across varying conditions (ito2022glutathionedegradationactivity pages 9-11, geuflores2011cytosolicγglutamylpeptidases pages 10-11).
Recent structural predictions and substrate-docking studies are beginning to reveal the molecular basis for GGP1's substrate recognition, although experimental crystal structures have not yet been reported. Understanding the structural determinants of substrate selectivity could inform efforts to engineer glucosinolate production in non-Brassicaceae species or to modulate plant sulfur metabolism for agricultural applications (ito2022glutathionedegradationactivity pages 11-12, ito2022glutathionedegradationactivity pages 12-13).
GGP1 (At4g30530, EC 3.4.19.16) is a cytosolic γ-glutamyl peptidase belonging to the C26 cysteine peptidase family that catalyzes hydrolysis of the γ-glutamyl bond in reduced glutathione and related glutathione conjugates. It functions in both primary sulfur metabolism (constitutive GSH degradation and amino acid recycling) and secondary sulfur metabolism (processing of GSH conjugates in glucosinolate and camalexin biosynthesis). The enzyme is localized to the cytosol, with particularly high expression in vascular tissues of leaves. Extensive experimental evidence from yeast complementation, enzyme kinetics, knockout mutant analyses, localization studies, and metabolomics supports these functional assignments. GGP1 exemplifies how a single enzyme with dual substrate specificity can integrate primary metabolic homeostasis with inducible defense responses, coordinating sulfur allocation according to physiological and environmental demands.
References
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(bhuiyan2020autocatalyticprocessingand pages 2-3): Nazmul H. Bhuiyan, Elden Rowland, Giulia Friso, Lalit Ponnala, Elena J. S. Michel, and Klaas J. van Wijk. Autocatalytic processing and substrate specificity of arabidopsis chloroplast glutamyl peptidase1[open]. Plant Physiology, 184:110-129, Jul 2020. URL: https://doi.org/10.1104/pp.20.00752, doi:10.1104/pp.20.00752. This article has 15 citations and is from a highest quality peer-reviewed journal.
(ito2022glutathionedegradationactivity pages 2-3): Takehiro Ito, Taisuke Kitaiwa, Kosuke Nishizono, Minori Umahashi, Shunsuke Miyaji, Shin‐ichiro Agake, Kana Kuwahara, Tadashi Yokoyama, Shinya Fushinobu, Akiko Maruyama‐Nakashita, Ryosuke Sugiyama, Muneo Sato, Jun Inaba, Masami Yokota Hirai, and Naoko Ohkama‐Ohtsu. Glutathione degradation activity of
(ito2022glutathionedegradationactivity pages 1-2): Takehiro Ito, Taisuke Kitaiwa, Kosuke Nishizono, Minori Umahashi, Shunsuke Miyaji, Shin‐ichiro Agake, Kana Kuwahara, Tadashi Yokoyama, Shinya Fushinobu, Akiko Maruyama‐Nakashita, Ryosuke Sugiyama, Muneo Sato, Jun Inaba, Masami Yokota Hirai, and Naoko Ohkama‐Ohtsu. Glutathione degradation activity of
(ito2022glutathionedegradationactivity pages 3-5): Takehiro Ito, Taisuke Kitaiwa, Kosuke Nishizono, Minori Umahashi, Shunsuke Miyaji, Shin‐ichiro Agake, Kana Kuwahara, Tadashi Yokoyama, Shinya Fushinobu, Akiko Maruyama‐Nakashita, Ryosuke Sugiyama, Muneo Sato, Jun Inaba, Masami Yokota Hirai, and Naoko Ohkama‐Ohtsu. Glutathione degradation activity of
(ito2022glutathionedegradationactivity pages 9-11): Takehiro Ito, Taisuke Kitaiwa, Kosuke Nishizono, Minori Umahashi, Shunsuke Miyaji, Shin‐ichiro Agake, Kana Kuwahara, Tadashi Yokoyama, Shinya Fushinobu, Akiko Maruyama‐Nakashita, Ryosuke Sugiyama, Muneo Sato, Jun Inaba, Masami Yokota Hirai, and Naoko Ohkama‐Ohtsu. Glutathione degradation activity of
(geuflores2011cytosolicγglutamylpeptidases pages 5-7): Fernando Geu-Flores, Morten Emil Møldrup, Christoph Böttcher, Carl Erik Olsen, Dierk Scheel, and Barbara Ann Halkier. Cytosolic γ-glutamyl peptidases process glutathione conjugates in the biosynthesis of glucosinolates and camalexin in arabidopsis. Jun 2011. URL: https://doi.org/10.1105/tpc.111.083998, doi:10.1105/tpc.111.083998. This article has 173 citations.
(geuflores2011cytosolicγglutamylpeptidases pages 8-10): Fernando Geu-Flores, Morten Emil Møldrup, Christoph Böttcher, Carl Erik Olsen, Dierk Scheel, and Barbara Ann Halkier. Cytosolic γ-glutamyl peptidases process glutathione conjugates in the biosynthesis of glucosinolates and camalexin in arabidopsis. Jun 2011. URL: https://doi.org/10.1105/tpc.111.083998, doi:10.1105/tpc.111.083998. This article has 173 citations.
(geuflores2011cytosolicγglutamylpeptidases pages 1-2): Fernando Geu-Flores, Morten Emil Møldrup, Christoph Böttcher, Carl Erik Olsen, Dierk Scheel, and Barbara Ann Halkier. Cytosolic γ-glutamyl peptidases process glutathione conjugates in the biosynthesis of glucosinolates and camalexin in arabidopsis. Jun 2011. URL: https://doi.org/10.1105/tpc.111.083998, doi:10.1105/tpc.111.083998. This article has 173 citations.
(ito2022glutathionedegradationactivity pages 12-13): Takehiro Ito, Taisuke Kitaiwa, Kosuke Nishizono, Minori Umahashi, Shunsuke Miyaji, Shin‐ichiro Agake, Kana Kuwahara, Tadashi Yokoyama, Shinya Fushinobu, Akiko Maruyama‐Nakashita, Ryosuke Sugiyama, Muneo Sato, Jun Inaba, Masami Yokota Hirai, and Naoko Ohkama‐Ohtsu. Glutathione degradation activity of
(geuflores2011cytosolicγglutamylpeptidases pages 4-5): Fernando Geu-Flores, Morten Emil Møldrup, Christoph Böttcher, Carl Erik Olsen, Dierk Scheel, and Barbara Ann Halkier. Cytosolic γ-glutamyl peptidases process glutathione conjugates in the biosynthesis of glucosinolates and camalexin in arabidopsis. Jun 2011. URL: https://doi.org/10.1105/tpc.111.083998, doi:10.1105/tpc.111.083998. This article has 173 citations.
(geuflores2011cytosolicγglutamylpeptidases pages 2-4): Fernando Geu-Flores, Morten Emil Møldrup, Christoph Böttcher, Carl Erik Olsen, Dierk Scheel, and Barbara Ann Halkier. Cytosolic γ-glutamyl peptidases process glutathione conjugates in the biosynthesis of glucosinolates and camalexin in arabidopsis. Jun 2011. URL: https://doi.org/10.1105/tpc.111.083998, doi:10.1105/tpc.111.083998. This article has 173 citations.
(ito2022glutathionedegradationactivity pages 6-7): Takehiro Ito, Taisuke Kitaiwa, Kosuke Nishizono, Minori Umahashi, Shunsuke Miyaji, Shin‐ichiro Agake, Kana Kuwahara, Tadashi Yokoyama, Shinya Fushinobu, Akiko Maruyama‐Nakashita, Ryosuke Sugiyama, Muneo Sato, Jun Inaba, Masami Yokota Hirai, and Naoko Ohkama‐Ohtsu. Glutathione degradation activity of
(geuflores2011cytosolicγglutamylpeptidases pages 7-8): Fernando Geu-Flores, Morten Emil Møldrup, Christoph Böttcher, Carl Erik Olsen, Dierk Scheel, and Barbara Ann Halkier. Cytosolic γ-glutamyl peptidases process glutathione conjugates in the biosynthesis of glucosinolates and camalexin in arabidopsis. Jun 2011. URL: https://doi.org/10.1105/tpc.111.083998, doi:10.1105/tpc.111.083998. This article has 173 citations.
(ito2022glutathionedegradationactivity pages 7-8): Takehiro Ito, Taisuke Kitaiwa, Kosuke Nishizono, Minori Umahashi, Shunsuke Miyaji, Shin‐ichiro Agake, Kana Kuwahara, Tadashi Yokoyama, Shinya Fushinobu, Akiko Maruyama‐Nakashita, Ryosuke Sugiyama, Muneo Sato, Jun Inaba, Masami Yokota Hirai, and Naoko Ohkama‐Ohtsu. Glutathione degradation activity of
(ito2022glutathionedegradationactivity pages 8-9): Takehiro Ito, Taisuke Kitaiwa, Kosuke Nishizono, Minori Umahashi, Shunsuke Miyaji, Shin‐ichiro Agake, Kana Kuwahara, Tadashi Yokoyama, Shinya Fushinobu, Akiko Maruyama‐Nakashita, Ryosuke Sugiyama, Muneo Sato, Jun Inaba, Masami Yokota Hirai, and Naoko Ohkama‐Ohtsu. Glutathione degradation activity of
(geuflores2011cytosolicγglutamylpeptidases pages 10-11): Fernando Geu-Flores, Morten Emil Møldrup, Christoph Böttcher, Carl Erik Olsen, Dierk Scheel, and Barbara Ann Halkier. Cytosolic γ-glutamyl peptidases process glutathione conjugates in the biosynthesis of glucosinolates and camalexin in arabidopsis. Jun 2011. URL: https://doi.org/10.1105/tpc.111.083998, doi:10.1105/tpc.111.083998. This article has 173 citations.