Isoleucine degradation
WikiPathways:WP178
Isoleucine degradation converts L-isoleucine to (S)-3-methyl-2-oxopentanoate, 2-methylbutanal, and 2-methylbutanol in Saccharomyces cerevisiae.
- Pathway type
- amino acid degradation
- Organism scope
Pathway network
27 nodes · 35 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
- Solid arrow: mechanistic relation
- Dashed arrow: membership, location or cofactor relation
Components and activities
| Node | Kind or role | Source direction |
|---|---|---|
Saccharomyces cerevisiaeNCBITaxon:4932 | taxon | |
L-isoleucineCHEBI:58045 | small molecule | |
BAT2SGD:S000003909 | protein | |
2-methylbutanalCHEBI:16182 | small molecule | |
NAD(1-)CHEBI:57540 | small molecule | |
BAT1SGD:S000001251 | protein | |
NADH(2-)CHEBI:57945 | small molecule | |
PDC1SGD:S000004034 | protein | |
L-glutamate(1-)CHEBI:29985 | small molecule | |
ARO10SGD:S000002788 | protein | |
PDC6SGD:S000003319 | protein | |
hydronCHEBI:15378 | small molecule | |
2-oxoglutarate(2-)CHEBI:16810 | small molecule | |
PDC5SGD:S000004124 | protein | |
2-methylbutanolCHEBI:48945 | small molecule | |
SFA1SGD:S000002327 | protein | |
carbon dioxideCHEBI:16526 | small molecule | |
(S)-3-methyl-2-oxopentanoateCHEBI:35146 | small molecule | |
ADH5SGD:S000000349 | protein | |
ADH4SGD:S000003225 | protein | |
pyridoxal 5'-phosphate(2-)CHEBI:597326 | cofactor | |
magnesium(2+)CHEBI:18420 | cofactor | |
thiamine(1+) diphosphate(3-)CHEBI:58937 | cofactor | |
zinc(2+)CHEBI:29105 | cofactor | |
iron(2+)CHEBI:29033 | cofactor | |
L-isoleucine to (S)-3-methyl-2-oxopentanoate GPML interactionWikiPathways:WP178/id59c25f71 | molecular activity | left to right |
2-methylbutanal to 2-methylbutanol GPML interactionWikiPathways:WP178/idbcd10869 | molecular activity | left to right |
(S)-3-methyl-2-oxopentanoate to 2-methylbutanal GPML interactionWikiPathways:WP178/idf1c4befb | molecular activity | left to right |
Mechanistic edges
| Subject | Predicate and description | Object | Evidence |
|---|---|---|---|
L-isoleucineCHEBI:58045 | consumes | L-isoleucine to (S)-3-methyl-2-oxopentanoate GPML interactionWikiPathways:WP178/id59c25f71 |
|
L-isoleucine to (S)-3-methyl-2-oxopentanoate GPML interactionWikiPathways:WP178/id59c25f71 | produces | (S)-3-methyl-2-oxopentanoateCHEBI:35146 |
|
2-methylbutanalCHEBI:16182 | consumes | 2-methylbutanal to 2-methylbutanol GPML interactionWikiPathways:WP178/idbcd10869 |
|
2-methylbutanal to 2-methylbutanol GPML interactionWikiPathways:WP178/idbcd10869 | produces | 2-methylbutanolCHEBI:48945 |
|
(S)-3-methyl-2-oxopentanoateCHEBI:35146 | consumes | (S)-3-methyl-2-oxopentanoate to 2-methylbutanal GPML interactionWikiPathways:WP178/idf1c4befb |
|
(S)-3-methyl-2-oxopentanoate to 2-methylbutanal GPML interactionWikiPathways:WP178/idf1c4befb | produces | 2-methylbutanalCHEBI:16182 |
|
(S)-3-methyl-2-oxopentanoate to 2-methylbutanal GPML interactionWikiPathways:WP178/idf1c4befb | produces | carbon dioxideCHEBI:16526 |
|
SFA1SGD:S000002327 | catalyzes | 2-methylbutanal to 2-methylbutanol GPML interactionWikiPathways:WP178/idbcd10869 |
|
ADH5SGD:S000000349 | catalyzes | 2-methylbutanal to 2-methylbutanol GPML interactionWikiPathways:WP178/idbcd10869 |
|
ADH4SGD:S000003225 | catalyzes | 2-methylbutanal to 2-methylbutanol GPML interactionWikiPathways:WP178/idbcd10869 |
|
BAT2SGD:S000003909 | catalyzes | L-isoleucine to (S)-3-methyl-2-oxopentanoate GPML interactionWikiPathways:WP178/id59c25f71 |
|
BAT1SGD:S000001251 | catalyzes | L-isoleucine to (S)-3-methyl-2-oxopentanoate GPML interactionWikiPathways:WP178/id59c25f71 |
|
NADH(2-)CHEBI:57945 | consumes | 2-methylbutanal to 2-methylbutanol GPML interactionWikiPathways:WP178/idbcd10869 |
|
2-methylbutanal to 2-methylbutanol GPML interactionWikiPathways:WP178/idbcd10869 | produces | NAD(1-)CHEBI:57540 |
|
PDC1SGD:S000004034 | catalyzes | (S)-3-methyl-2-oxopentanoate to 2-methylbutanal GPML interactionWikiPathways:WP178/idf1c4befb |
|
ARO10SGD:S000002788 | catalyzes | (S)-3-methyl-2-oxopentanoate to 2-methylbutanal GPML interactionWikiPathways:WP178/idf1c4befb |
|
PDC6SGD:S000003319 | catalyzes | (S)-3-methyl-2-oxopentanoate to 2-methylbutanal GPML interactionWikiPathways:WP178/idf1c4befb |
|
PDC5SGD:S000004124 | catalyzes | (S)-3-methyl-2-oxopentanoate to 2-methylbutanal GPML interactionWikiPathways:WP178/idf1c4befb |
|
2-oxoglutarate(2-)CHEBI:16810 | consumes | L-isoleucine to (S)-3-methyl-2-oxopentanoate GPML interactionWikiPathways:WP178/id59c25f71 |
|
L-isoleucine to (S)-3-methyl-2-oxopentanoate GPML interactionWikiPathways:WP178/id59c25f71 | produces | L-glutamate(1-)CHEBI:29985 |
|
hydronCHEBI:15378 | consumes | (S)-3-methyl-2-oxopentanoate to 2-methylbutanal GPML interactionWikiPathways:WP178/idf1c4befb |
|
BAT2SGD:S000003909 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: not specified | pyridoxal 5'-phosphate(2-)CHEBI:597326 |
|
BAT1SGD:S000001251 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. Reviewed source qualification: Disputed growth phenotypes do not address PLP binding; retain the similarity-based PLP annotation. UniProt evidence: ECO:0000250 (UniProtKB:P0AB80) | pyridoxal 5'-phosphate(2-)CHEBI:597326 |
|
PDC1SGD:S000004034 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000269 (PubMed:10651824) Binds 1 Mg(2+) per subunit. UniProt note evidence: ECO:0000269 (PubMed:10651824) | magnesium(2+)CHEBI:18420 |
|
PDC1SGD:S000004034 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000269 (PubMed:10651824) Binds 1 thiamine pyrophosphate per subunit. UniProt note evidence: ECO:0000269 (PubMed:10651824) | thiamine(1+) diphosphate(3-)CHEBI:58937 |
|
ARO10SGD:S000002788 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000250 Binds 1 Mg(2+) per subunit. UniProt note evidence: ECO:0000250 | magnesium(2+)CHEBI:18420 |
|
ARO10SGD:S000002788 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000250 Binds 1 thiamine pyrophosphate per subunit. UniProt note evidence: ECO:0000250 | thiamine(1+) diphosphate(3-)CHEBI:58937 |
|
PDC6SGD:S000003319 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000250 (UniProtKB:P06169) Binds 1 Mg(2+) per subunit. UniProt note evidence: ECO:0000250 (UniProtKB:P06169) | magnesium(2+)CHEBI:18420 |
|
PDC6SGD:S000003319 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000250 (UniProtKB:P06169) Binds 1 thiamine pyrophosphate per subunit. UniProt note evidence: ECO:0000250 (UniProtKB:P06169) | thiamine(1+) diphosphate(3-)CHEBI:58937 |
|
PDC5SGD:S000004124 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000250 (UniProtKB:P06169) Binds 1 Mg(2+) per subunit. UniProt note evidence: ECO:0000250 (UniProtKB:P06169) | magnesium(2+)CHEBI:18420 |
|
PDC5SGD:S000004124 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000250 (UniProtKB:P06169) Binds 1 thiamine pyrophosphate per subunit. UniProt note evidence: ECO:0000250 (UniProtKB:P06169) | thiamine(1+) diphosphate(3-)CHEBI:58937 |
|
SFA1SGD:S000002327 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000250 (UniProtKB:P06525) Binds 2 Zn(2+) ions per subunit. UniProt note evidence: ECO:0000250 (UniProtKB:P06525) | zinc(2+)CHEBI:29105 |
|
ADH5SGD:S000000349 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000250 (UniProtKB:P00330) Binds 2 Zn(2+) ions per subunit. UniProt note evidence: ECO:0000250 (UniProtKB:P00330) | zinc(2+)CHEBI:29105 |
|
ADH4SGD:S000003225 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000269 (PubMed:3282541) Zinc. May bind iron when zinc levels are limiting. UniProt note evidence: ECO:0000269 (PubMed:3282541) | zinc(2+)CHEBI:29105 |
|
ADH4SGD:S000003225 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000269 (PubMed:3282541) Zinc. May bind iron when zinc levels are limiting. UniProt note evidence: ECO:0000269 (PubMed:3282541) | iron(2+)CHEBI:29033 |
|
References
WikiPathways:WP178WP178 native structured pathway source (source version: WP178_r140283)DOI:10.1128/AEM.01675-12Substrate Specificity of Thiamine Pyrophosphate-Dependent 2-Oxo-Acid Decarboxylases in Saccharomyces cerevisiaeUniProtKB:P47176UniProtKB P47176 cofactor annotations (source version: 2026_03)UniProtKB:P38891UniProtKB P38891 cofactor annotations (source version: 2026_03)UniProtKB:P06169UniProtKB P06169 cofactor annotations (source version: 2026_03)UniProtKB:Q06408UniProtKB Q06408 cofactor annotations (source version: 2026_03)UniProtKB:P26263UniProtKB P26263 cofactor annotations (source version: 2026_03)UniProtKB:P16467UniProtKB P16467 cofactor annotations (source version: 2026_03)UniProtKB:P32771UniProtKB P32771 cofactor annotations (source version: 2026_03)UniProtKB:P38113UniProtKB P38113 cofactor annotations (source version: 2026_03)UniProtKB:P10127UniProtKB P10127 cofactor annotations (source version: 2026_03)
Curation history
- Codex
- EDIT — Review complete causal graph against native sources and correct unsupported or omitted relationships
Restored catalysts and cosubstrates. Excluded THI3 catalytic assignment: individual enzyme assays in DOI10.1128/AEM.01675-12 found no activity. No subcellular location inferred from isozyme identity alone. Every native record was inspected; see reports/causal-graph-diagram-review.json for native-object counts, exclusions and identity corrections. Semantic validation and native GraphId locator checks passed; authority snapshots and full corpus gates are coordinated separately.
- EDIT — Review complete causal graph against native sources and correct unsupported or omitted relationships