glutathione degradation
gomodel:YeastPathways_PWYQT-4432
Glutathione degradation uses ECM38 to transfer glutathione's gamma-glutamyl moiety to a proteinogenic amino acid, forming L-cysteinylglycine and an L-gamma-glutamyl-L-amino acid, then uses DUG1 to hydrolyze L-cysteinylglycine to L-cysteine and glycine in Saccharomyces cerevisiae S288C.
- Pathway type
- glutathione degradation
- Organism scope
Pathway network
19 nodes · 20 asserted directed edges
Arrows show recorded subject → object relationships, not necessarily metabolic flow. Select a node for details or an arrow for evidence. Scroll, zoom or find a node to explore.
- Reaction / activity
- Chemical / cofactor
- Protein / complex
- Cell / process context
- Solid arrow: mechanistic relation
- Dashed arrow: membership, location or cofactor relation
Components and activities
| Node | Kind or role | Source direction |
|---|---|---|
Saccharomyces cerevisiae S288CNCBITaxon:559292 | taxon | |
glutathione catabolic processGO:0006751 | biological process | |
L-cysteinylglycine zwitterionCHEBI:61694 | small molecule | |
cytosolGO:0005829 | cellular component | |
waterCHEBI:15377 | small molecule | |
glutathioneCHEBI:16856 | small molecule | |
DUG1 ScerSGD:S000001940 | protein | |
L-cysteine zwitterionCHEBI:35235 | small molecule | |
L-gamma-glutamyl-L-amino acid(1-)CHEBI:71304 | small molecule | |
ECM38 ScerSGD:S000004290 | protein | |
proteinogenic amino acidCHEBI:83813 | small molecule | |
glycine zwitterionCHEBI:57305 | small molecule | |
cytoplasmGO:0005737 | cellular component | |
mitochondrionGO:0005739 | cellular component | |
vacuolar membraneGO:0005774 | cellular component | |
vacuoleGO:0005773 | cellular component | |
zinc(2+)CHEBI:29105 | cofactor | |
manganese(2+)CHEBI:29035 | cofactor | |
glutathione gamma-glutamate hydrolasegomodel:RXN-6601 | molecular activity | |
metallodipeptidase activitygomodel:RXN-6622 | molecular activity |
Mechanistic edges
| Subject | Predicate and description | Object | Evidence |
|---|---|---|---|
glutathione gamma-glutamate hydrolasegomodel:RXN-6601 | part_of | glutathione catabolic processGO:0006751 |
|
glutathione gamma-glutamate hydrolasegomodel:RXN-6601 | has_output | L-cysteinylglycine zwitterionCHEBI:61694 |
|
metallodipeptidase activitygomodel:RXN-6622 | occurs_in | cytosolGO:0005829 |
|
metallodipeptidase activitygomodel:RXN-6622 | has_input | waterCHEBI:15377 |
|
glutathione gamma-glutamate hydrolasegomodel:RXN-6601 | has_input | glutathioneCHEBI:16856 |
|
metallodipeptidase activitygomodel:RXN-6622 | has_input | L-cysteinylglycine zwitterionCHEBI:61694 |
|
DUG1 ScerSGD:S000001940 | enables | metallodipeptidase activitygomodel:RXN-6622 |
|
metallodipeptidase activitygomodel:RXN-6622 | has_output | L-cysteine zwitterionCHEBI:35235 |
|
glutathione gamma-glutamate hydrolasegomodel:RXN-6601 | has_output | L-gamma-glutamyl-L-amino acid(1-)CHEBI:71304 |
|
metallodipeptidase activitygomodel:RXN-6622 | part_of | glutathione catabolic processGO:0006751 |
|
ECM38 ScerSGD:S000004290 | enables | glutathione gamma-glutamate hydrolasegomodel:RXN-6601 |
|
glutathione gamma-glutamate hydrolasegomodel:RXN-6601 | provides_input_for | metallodipeptidase activitygomodel:RXN-6622 |
|
glutathione gamma-glutamate hydrolasegomodel:RXN-6601 | has_input | proteinogenic amino acidCHEBI:83813 |
|
metallodipeptidase activitygomodel:RXN-6622 | has_output | glycine zwitterionCHEBI:57305 |
|
DUG1 ScerSGD:S000001940 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:14562095); ECO:0000269 (PubMed:17179087) | cytoplasmGO:0005737 |
|
DUG1 ScerSGD:S000001940 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:16823961) | mitochondrionGO:0005739 |
|
ECM38 ScerSGD:S000004290 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:11672438); ECO:0000269 (PubMed:6143552); ECO:0000269 (PubMed:6143574) Topology: Single-pass type II membrane protein. | vacuolar membraneGO:0005774 |
|
glutathione gamma-glutamate hydrolasegomodel:RXN-6601 | occurs_in Activity compartment supported by an inspected functional annotation. ECO:0000269 (PubMed:11672438). Alternative isoenzymes may function elsewhere. | vacuoleGO:0005773 |
|
DUG1 ScerSGD:S000001940 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000269 (PubMed:19346245) | zinc(2+)CHEBI:29105 |
|
DUG1 ScerSGD:S000001940 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000269 (PubMed:19346245) | manganese(2+)CHEBI:29035 |
|
References
gomodel:YeastPathways_PWYQT-4432GO-CAM glutathione degradation model YeastPathways_PWYQT-4432 (source version: Pinned Noctua JSON archive; model date 2026-08-03; member ./YeastPathways_PWYQT-4432.json)UniProtKB:P43616Reviewed UniProtKB P43616 location annotations (source version: UniProt release 2026_03)UniProtKB:Q05902Reviewed UniProtKB Q05902 location annotations (source version: UniProt release 2026_03)
Curation history
- Codex; review-causal-graph; Reviewed every native GO-CAM fact; preserved precise input/output, causal, location, membership and complex-part relations with traceable structured source evidence. Kept distinct generic physical instances and recorded source-scope exclusions in the cohort review ledger.
- Codex
- EDIT — Audit causal activity compartments and preserve scoped protein location evidence
Reviewed all 2 activity location assignments and 2 mapped physical proteins against reviewed S288C UniProt release2026_03 location/function/caution batch SHA256 95f72dcc644358c480e0e59f996cf88533558b5fa4256460a030e0a1eaf9678d. Added 4 independently supported location edges and quarantined 1 generic cytosol source assertions. Mapped physical protein locations via exact SGD cross-references; retained source ECO grades, molecular form and conditional notes. Physical protein location alone never generates activity location. Explicitly inspected functional assertions support bounded activity projections. Every original activity location and exclusion is recorded in reports/causal_graph_review/gocam-location-review.json. No independent location annotation is treated as an evidence gap, not a negative result. Cytoplasm is not narrowed to cytosol. Microsome fractions are not projected as in-vivo organelles. Semantic validation passed all85 records;4 independent source-role acceptance tests passed.
- EDIT — Audit causal activity compartments and preserve scoped protein location evidence