LeuD is the required small swivel subunit of the LeuC-LeuD 3-isopropylmalate dehydratase. The heterodimer isomerizes 2-isopropylmalate to 3-isopropylmalate in the second dedicated reaction of L-leucine biosynthesis.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003861 3-isopropylmalate dehydratase activity | IEA GO_REF:0000120 | ACCEPT | Summary: LeuD is a required, non-catalytic subunit that contributes to the heterodimeric enzyme carrying this activity. Reason: EC 4.2.1.33, HAMAP, and LeuD-specific family assignments agree. Because LeuD has no independent catalytic activity, `contributes_to` is a better qualifier than the machine-sourced `enables` for this subunit. Supporting Evidence: file:PSEPK/leuD/leuD-uniprot.txt Full=3-isopropylmalate dehydratase small subunit file:PSEPK/leuD/leuD-uniprot.txt Heterodimer of LeuC and LeuD. file:PSEPK/leuD/leuD-deep-research-openscientist.md It has **no independent catalytic activity**; instead it forms an **obligate 1:1 heterodimer with the large subunit LeuC (PP_1985)**. |
| GO:0009098 L-leucine biosynthetic process | IEA GO_REF:0000120 | ACCEPT | Summary: LeuD participates in the second leucine-specific step. Reason: UniProt places the LeuC-LeuD heterodimer at step 2 of 4. |
| GO:0009316 3-isopropylmalate dehydratase complex | IEA GO_REF:0000002 | ACCEPT | Summary: This accurately records the defining LeuC-LeuD heterodimer membership. Reason: LeuD has no independent catalytic activity; its required role is realized as the small subunit of this complex. Supporting Evidence: file:PSEPK/leuD/leuD-uniprot.txt Heterodimer of LeuC and LeuD. |
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