L-homocysteine biosynthesis
gomodel:YeastPathways_PWY-5344
L-homocysteine biosynthesis in Saccharomyces cerevisiae S288C uses MET2 to acetylate L-homoserine with acetyl-CoA, forming O-acetyl-L-homoserine and coenzyme A, then uses MET17 to condense O-acetyl-L-homoserine with hydrogen sulfide to produce L-homocysteine, acetate, and hydron.
- Pathway type
- amino acid biosynthesis
- Organism scope
Pathway network
16 nodes · 19 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 | |
acetateCHEBI:30089 | small molecule | |
O-acetyl-L-homoserine zwitterionCHEBI:57716 | small molecule | |
MET2 ScerSGD:S000005221 | protein | |
L-homoserine zwitterionCHEBI:57476 | small molecule | |
hydronCHEBI:15378 | small molecule | |
acetyl-CoA(4-)CHEBI:57288 | small molecule | |
hydrogen sulfideCHEBI:16136 | small molecule | |
L-homocysteine biosynthetic processGO:0071269 | biological process | |
L-homocysteine zwitterionCHEBI:58199 | small molecule | |
cytosolGO:0005829 | cellular component | |
coenzyme A(4-)CHEBI:57287 | small molecule | |
MET17 ScerSGD:S000004294 | protein | |
cytoplasmGO:0005737 | cellular component | |
pyridoxal 5'-phosphate(2-)CHEBI:597326 | cofactor | |
O-acetyl-L-homoserine + hydrogen sulfide -> L-homocysteine + acetate + H+gomodel:ACETYLHOMOSER-CYS-RXN | molecular activity | |
L-homoserine + acetyl-CoA -> O-acetyl-L-homoserine + coenzyme Agomodel:HOMOSERINE-O-ACETYLTRANSFERASE-RXN | molecular activity |
Mechanistic edges
| Subject | Predicate and description | Object | Evidence |
|---|---|---|---|
O-acetyl-L-homoserine + hydrogen sulfide -> L-homocysteine + acetate + H+gomodel:ACETYLHOMOSER-CYS-RXN | has_output | acetateCHEBI:30089 |
|
L-homoserine + acetyl-CoA -> O-acetyl-L-homoserine + coenzyme Agomodel:HOMOSERINE-O-ACETYLTRANSFERASE-RXN | has_output | O-acetyl-L-homoserine zwitterionCHEBI:57716 |
|
MET2 ScerSGD:S000005221 | enables | L-homoserine + acetyl-CoA -> O-acetyl-L-homoserine + coenzyme Agomodel:HOMOSERINE-O-ACETYLTRANSFERASE-RXN |
|
O-acetyl-L-homoserine + hydrogen sulfide -> L-homocysteine + acetate + H+gomodel:ACETYLHOMOSER-CYS-RXN | has_input | O-acetyl-L-homoserine zwitterionCHEBI:57716 |
|
L-homoserine + acetyl-CoA -> O-acetyl-L-homoserine + coenzyme Agomodel:HOMOSERINE-O-ACETYLTRANSFERASE-RXN | has_input | L-homoserine zwitterionCHEBI:57476 |
|
O-acetyl-L-homoserine + hydrogen sulfide -> L-homocysteine + acetate + H+gomodel:ACETYLHOMOSER-CYS-RXN | has_output | hydronCHEBI:15378 |
|
L-homoserine + acetyl-CoA -> O-acetyl-L-homoserine + coenzyme Agomodel:HOMOSERINE-O-ACETYLTRANSFERASE-RXN | has_input | acetyl-CoA(4-)CHEBI:57288 |
|
O-acetyl-L-homoserine + hydrogen sulfide -> L-homocysteine + acetate + H+gomodel:ACETYLHOMOSER-CYS-RXN | has_input | hydrogen sulfideCHEBI:16136 |
|
L-homoserine + acetyl-CoA -> O-acetyl-L-homoserine + coenzyme Agomodel:HOMOSERINE-O-ACETYLTRANSFERASE-RXN | part_of | L-homocysteine biosynthetic processGO:0071269 |
|
O-acetyl-L-homoserine + hydrogen sulfide -> L-homocysteine + acetate + H+gomodel:ACETYLHOMOSER-CYS-RXN | has_output | L-homocysteine zwitterionCHEBI:58199 |
|
O-acetyl-L-homoserine + hydrogen sulfide -> L-homocysteine + acetate + H+gomodel:ACETYLHOMOSER-CYS-RXN | occurs_in | cytosolGO:0005829 |
|
L-homoserine + acetyl-CoA -> O-acetyl-L-homoserine + coenzyme Agomodel:HOMOSERINE-O-ACETYLTRANSFERASE-RXN | has_output | coenzyme A(4-)CHEBI:57287 |
|
O-acetyl-L-homoserine + hydrogen sulfide -> L-homocysteine + acetate + H+gomodel:ACETYLHOMOSER-CYS-RXN | part_of | L-homocysteine biosynthetic processGO:0071269 |
|
MET17 ScerSGD:S000004294 | enables | O-acetyl-L-homoserine + hydrogen sulfide -> L-homocysteine + acetate + H+gomodel:ACETYLHOMOSER-CYS-RXN |
|
L-homoserine + acetyl-CoA -> O-acetyl-L-homoserine + coenzyme Agomodel:HOMOSERINE-O-ACETYLTRANSFERASE-RXN | provides_input_for | O-acetyl-L-homoserine + hydrogen sulfide -> L-homocysteine + acetate + H+gomodel:ACETYLHOMOSER-CYS-RXN |
|
L-homoserine + acetyl-CoA -> O-acetyl-L-homoserine + coenzyme Agomodel:HOMOSERINE-O-ACETYLTRANSFERASE-RXN | occurs_in | cytosolGO:0005829 |
|
MET2 ScerSGD:S000005221 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:11914276); ECO:0000269 (PubMed:14562095) | cytoplasmGO:0005737 |
|
MET17 ScerSGD:S000004294 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:11914276) | cytoplasmGO:0005737 |
|
MET17 ScerSGD:S000004294 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000269 (PubMed:4609980); ECO:0000269 (PubMed:4947307); ECO:0000269 (PubMed:7765825); ECO:0000269 (PubMed:795806) | pyridoxal 5'-phosphate(2-)CHEBI:597326 |
|
References
gomodel:YeastPathways_PWY-5344SGD GO-CAM L-homocysteine biosynthesis pathway PWY-5344 (source version: Pinned Noctua JSON archive; model date 2026-07-31; member ./YeastPathways_PWY-5344.json)UniProtKB:P08465Reviewed UniProtKB P08465 location annotations (source version: UniProt release 2026_03)UniProtKB:P06106Reviewed UniProtKB P06106 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 2 independently supported location edges and quarantined 0 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