pyruvate decarboxylation to acetyl CoA
gomodel:YeastPathways_PYRUVDEHYD-PWY
Pyruvate decarboxylation to acetyl CoA in Saccharomyces cerevisiae S288C uses pyruvate dehydrogenase activities to transfer acetyl groups through lipoyl-lysine intermediates, form acetyl-CoA, and regenerate oxidized lipoyl cofactor while reducing NAD(+) to NADH.
- Pathway type
- central carbon metabolism
- Organism scope
Pathway network
25 nodes · 36 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 | |
pyruvateCHEBI:15361 | small molecule | |
pyruvate decarboxylation to acetyl-CoAGO:0006086 | biological process | |
hydronCHEBI:15378 | small molecule | |
carbon dioxideCHEBI:16526 | small molecule | |
Enzyme N6-(lipoyl)lysineCHEBI:80218 | small molecule | |
cytosolGO:0005829 | cellular component | |
[Dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysineCHEBI:80404 | small molecule | |
Enzyme N6-(dihydrolipoyl)lysineCHEBI:80219 | small molecule | |
LAT1 ScerSGD:S000005015 | protein | |
acetyl-CoA(4-)CHEBI:57288 | small molecule | |
LPD1 ScerSGD:S000001876 | protein | |
NAD(1-)CHEBI:57540 | small molecule | |
PDB1 ScerSGD:S000000425 | protein | |
NADH(2-)CHEBI:57945 | small molecule | |
PDA1 ScerSGD:S000000980 | protein | |
coenzyme A(4-)CHEBI:57287 | small molecule | |
mitochondrial matrixGO:0005759 | cellular component | |
(R)-lipoateCHEBI:83088 | cofactor | |
FAD(3-)CHEBI:57692 | cofactor | |
thiamine(1+) diphosphate(3-)CHEBI:58937 | cofactor | |
magnesium(2+)CHEBI:18420 | cofactor | |
a [pyruvate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine + NAD+ -> a [pyruvate dehydrogenase E2 protein] N6-lipoyl-L-lysine + NADH + H+gomodel:RXN0-1132 | molecular activity | |
acetyl-CoA + a [pyruvate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine <- a [pyruvate dehydrogenase E2 protein] N6-S-acetyldihydrolipoyl-L-lysine + coenzyme Agomodel:RXN0-1133 | molecular activity | |
pyruvate + a [pyruvate dehydrogenase E2 protein] N6-lipoyl-L-lysine + H+ -> a [pyruvate dehydrogenase E2 protein] N6-S-acetyldihydrolipoyl-L-lysine + CO2gomodel:RXN0-1134 | molecular activity | |
pyruvate dehydrogenase (acetyl-transferring) activitygomodel:YeastPathways_PYRUVDEHYD-PWY/6a4c244800000320 | molecular activity |
Mechanistic edges
| Subject | Predicate and description | Object | Evidence |
|---|---|---|---|
pyruvate dehydrogenase (acetyl-transferring) activitygomodel:YeastPathways_PYRUVDEHYD-PWY/6a4c244800000320 | has_input | pyruvateCHEBI:15361 |
|
pyruvate + a [pyruvate dehydrogenase E2 protein] N6-lipoyl-L-lysine + H+ -> a [pyruvate dehydrogenase E2 protein] N6-S-acetyldihydrolipoyl-L-lysine + CO2gomodel:RXN0-1134 | part_of | pyruvate decarboxylation to acetyl-CoAGO:0006086 |
|
pyruvate dehydrogenase (acetyl-transferring) activitygomodel:YeastPathways_PYRUVDEHYD-PWY/6a4c244800000320 | has_input | hydronCHEBI:15378 |
|
pyruvate + a [pyruvate dehydrogenase E2 protein] N6-lipoyl-L-lysine + H+ -> a [pyruvate dehydrogenase E2 protein] N6-S-acetyldihydrolipoyl-L-lysine + CO2gomodel:RXN0-1134 | has_output | carbon dioxideCHEBI:16526 |
|
a [pyruvate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine + NAD+ -> a [pyruvate dehydrogenase E2 protein] N6-lipoyl-L-lysine + NADH + H+gomodel:RXN0-1132 | part_of | pyruvate decarboxylation to acetyl-CoAGO:0006086 |
|
pyruvate dehydrogenase (acetyl-transferring) activitygomodel:YeastPathways_PYRUVDEHYD-PWY/6a4c244800000320 | has_input | Enzyme N6-(lipoyl)lysineCHEBI:80218 |
|
pyruvate + a [pyruvate dehydrogenase E2 protein] N6-lipoyl-L-lysine + H+ -> a [pyruvate dehydrogenase E2 protein] N6-S-acetyldihydrolipoyl-L-lysine + CO2gomodel:RXN0-1134 | has_input | Enzyme N6-(lipoyl)lysineCHEBI:80218 |
|
pyruvate dehydrogenase (acetyl-transferring) activitygomodel:YeastPathways_PYRUVDEHYD-PWY/6a4c244800000320 | part_of | pyruvate decarboxylation to acetyl-CoAGO:0006086 |
|
pyruvate dehydrogenase (acetyl-transferring) activitygomodel:YeastPathways_PYRUVDEHYD-PWY/6a4c244800000320 | has_output | [Dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysineCHEBI:80404 |
|
a [pyruvate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine + NAD+ -> a [pyruvate dehydrogenase E2 protein] N6-lipoyl-L-lysine + NADH + H+gomodel:RXN0-1132 | has_input | Enzyme N6-(dihydrolipoyl)lysineCHEBI:80219 |
|
acetyl-CoA + a [pyruvate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine <- a [pyruvate dehydrogenase E2 protein] N6-S-acetyldihydrolipoyl-L-lysine + coenzyme Agomodel:RXN0-1133 | part_of | pyruvate decarboxylation to acetyl-CoAGO:0006086 |
|
pyruvate dehydrogenase (acetyl-transferring) activitygomodel:YeastPathways_PYRUVDEHYD-PWY/6a4c244800000320 | has_output | carbon dioxideCHEBI:16526 |
|
LAT1 ScerSGD:S000005015 | enables | acetyl-CoA + a [pyruvate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine <- a [pyruvate dehydrogenase E2 protein] N6-S-acetyldihydrolipoyl-L-lysine + coenzyme Agomodel:RXN0-1133 |
|
pyruvate + a [pyruvate dehydrogenase E2 protein] N6-lipoyl-L-lysine + H+ -> a [pyruvate dehydrogenase E2 protein] N6-S-acetyldihydrolipoyl-L-lysine + CO2gomodel:RXN0-1134 | has_input | hydronCHEBI:15378 |
|
acetyl-CoA + a [pyruvate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine <- a [pyruvate dehydrogenase E2 protein] N6-S-acetyldihydrolipoyl-L-lysine + coenzyme Agomodel:RXN0-1133 | has_output | acetyl-CoA(4-)CHEBI:57288 |
|
a [pyruvate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine + NAD+ -> a [pyruvate dehydrogenase E2 protein] N6-lipoyl-L-lysine + NADH + H+gomodel:RXN0-1132 | has_output | hydronCHEBI:15378 |
|
acetyl-CoA + a [pyruvate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine <- a [pyruvate dehydrogenase E2 protein] N6-S-acetyldihydrolipoyl-L-lysine + coenzyme Agomodel:RXN0-1133 | has_input | [Dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysineCHEBI:80404 |
|
LPD1 ScerSGD:S000001876 | enables | a [pyruvate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine + NAD+ -> a [pyruvate dehydrogenase E2 protein] N6-lipoyl-L-lysine + NADH + H+gomodel:RXN0-1132 |
|
a [pyruvate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine + NAD+ -> a [pyruvate dehydrogenase E2 protein] N6-lipoyl-L-lysine + NADH + H+gomodel:RXN0-1132 | has_output | Enzyme N6-(lipoyl)lysineCHEBI:80218 |
|
acetyl-CoA + a [pyruvate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine <- a [pyruvate dehydrogenase E2 protein] N6-S-acetyldihydrolipoyl-L-lysine + coenzyme Agomodel:RXN0-1133 | has_output | Enzyme N6-(dihydrolipoyl)lysineCHEBI:80219 |
|
a [pyruvate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine + NAD+ -> a [pyruvate dehydrogenase E2 protein] N6-lipoyl-L-lysine + NADH + H+gomodel:RXN0-1132 | has_input | NAD(1-)CHEBI:57540 |
|
PDB1 ScerSGD:S000000425 | enables | pyruvate dehydrogenase (acetyl-transferring) activitygomodel:YeastPathways_PYRUVDEHYD-PWY/6a4c244800000320 |
|
pyruvate + a [pyruvate dehydrogenase E2 protein] N6-lipoyl-L-lysine + H+ -> a [pyruvate dehydrogenase E2 protein] N6-S-acetyldihydrolipoyl-L-lysine + CO2gomodel:RXN0-1134 | has_input | pyruvateCHEBI:15361 |
|
a [pyruvate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine + NAD+ -> a [pyruvate dehydrogenase E2 protein] N6-lipoyl-L-lysine + NADH + H+gomodel:RXN0-1132 | has_output | NADH(2-)CHEBI:57945 |
|
pyruvate + a [pyruvate dehydrogenase E2 protein] N6-lipoyl-L-lysine + H+ -> a [pyruvate dehydrogenase E2 protein] N6-S-acetyldihydrolipoyl-L-lysine + CO2gomodel:RXN0-1134 | has_output | [Dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysineCHEBI:80404 |
|
PDA1 ScerSGD:S000000980 | enables | pyruvate + a [pyruvate dehydrogenase E2 protein] N6-lipoyl-L-lysine + H+ -> a [pyruvate dehydrogenase E2 protein] N6-S-acetyldihydrolipoyl-L-lysine + CO2gomodel:RXN0-1134 |
|
acetyl-CoA + a [pyruvate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine <- a [pyruvate dehydrogenase E2 protein] N6-S-acetyldihydrolipoyl-L-lysine + coenzyme Agomodel:RXN0-1133 | has_input | coenzyme A(4-)CHEBI:57287 |
|
LAT1 ScerSGD:S000005015 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:14562095) | mitochondrial matrixGO:0005759 |
|
LPD1 ScerSGD:S000001876 | located_in Physical protein location from reviewed UniProt. evidence code not specified by source | mitochondrial matrixGO:0005759 |
|
PDB1 ScerSGD:S000000425 | located_in Physical protein location from reviewed UniProt. evidence code not specified by source | mitochondrial matrixGO:0005759 |
|
PDA1 ScerSGD:S000000980 | located_in Physical protein location from reviewed UniProt. evidence code not specified by source | mitochondrial matrixGO:0005759 |
|
LAT1 ScerSGD:S000005015 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. Reviewed source qualification: The source describes a covalently attached cofactor moiety. Keep that bound-state qualification; no free cosubstrate consumption is inferred. UniProt evidence: not specified Binds 1 lipoyl cofactor covalently. UniProt note evidence: ECO:0000269 (PubMed:3050999) | (R)-lipoateCHEBI:83088 |
|
LPD1 ScerSGD:S000001876 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000269 (PubMed:9538259); ECO:0000269 (Reference:Ref.13) Binds 1 FAD per subunit. UniProt note evidence: ECO:0000269 (PubMed:9538259); ECO:0000269 (Reference:Ref.13) | FAD(3-)CHEBI:57692 |
|
PDB1 ScerSGD:S000000425 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000250 (UniProtKB:P11177) | thiamine(1+) diphosphate(3-)CHEBI:58937 |
|
PDA1 ScerSGD:S000000980 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000250 (UniProtKB:P08559) | thiamine(1+) diphosphate(3-)CHEBI:58937 |
|
PDA1 ScerSGD:S000000980 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000250 (UniProtKB:P08559) | magnesium(2+)CHEBI:18420 |
|
References
gomodel:YeastPathways_PYRUVDEHYD-PWYSGD GO-CAM pyruvate decarboxylation to acetyl CoA - imported from: Saccharomyces Genome Database (source version: Pinned Noctua JSON archive; model date 2026-07-07; member ./YeastPathways_PYRUVDEHYD-PWY.json)UniProtKB:P12695Reviewed UniProtKB P12695 location annotations (source version: UniProt release 2026_03)UniProtKB:P09624Reviewed UniProtKB P09624 location annotations (source version: UniProt release 2026_03)UniProtKB:P32473Reviewed UniProtKB P32473 location annotations (source version: UniProt release 2026_03)UniProtKB:P16387Reviewed UniProtKB P16387 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 4 activity location assignments and 4 mapped physical proteins against reviewed S288C UniProt release2026_03 location/function/caution batch SHA256 95f72dcc644358c480e0e59f996cf88533558b5fa4256460a030e0a1eaf9678d. Added 4 independently supported location edges and quarantined 4 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