Function
Processes
Locations
Supplies extracellular D-3-hydroxybutyrate to the catabolic reactions.
A reusable pathway for use of D-3-hydroxybutyrate as a carbon and energy source. D-3-hydroxybutyrate is oxidized to acetoacetate, acetoacetate is activated to acetoacetyl-CoA, and a thiolase can cleave acetoacetyl-CoA to acetyl-CoA. Organisms differ in the activation reaction: animal ketolysis generally uses a succinyl-CoA-dependent CoA transferase, whereas some bacteria use an ATP-dependent acetoacetate-CoA ligase. Substrate import is an optional upstream role for organisms that consume extracellular ketone bodies. Intracellular D-3-hydroxybutyrate released from storage-polymer metabolism can enter at the oxidation step. Pseudomonas putida KT2440 provides candidate exemplars for import, oxidation, and ATP-dependent activation; their pathway dominance and the terminal thiolase remain to be resolved experimentally.
This revision removes the previous mammal-only tissue framing and models the conserved chemistry with taxon-dependent acetoacetate-activation variants. CONCRETE denotes the defined reaction topology, while family participants keep the pathway reusable across taxa. KT2440 BhbP, HbdH, Aacs, and BktB are candidates grounded to exact UniProt accessions, not experimentally proven assignments. Storage-polymer-derived D-3-hydroxybutyrate is a possible intracellular entry in bacteria, but KT2440 is known primarily for medium-chain-length PHA and its substrate source here remains unresolved.
module.knowledge_gaps[0] · status
(0/1)module.knowledge_gaps[0] · provenance
(0/1)module.knowledge_gaps[1] · status
(0/1)module.knowledge_gaps[1] · provenance
(0/1)✗ none found
No MODULE:ketone_body_oxidation deep-research report alongside the module YAML.
✓ every leaf node grounds to a representative protein.
✓ every declared conforms_to bundle matches its template motif.
✓ every PRECEDES step chains, or its break is acknowledged via chaining_status.
5 complete review(s) · 0 with deep research · 1 missing review · 6 reviewed but lacking deep research
| Gene | Review | Complete | Deep research |
|---|---|---|---|
| aacs Q88IC8 | ✓ | ✓ | ✗ |
| ACAT1 P24752 | ✓ | 43/49 | ✗ |
| BDH1 Q02338 | ✓ | ✓ | ✗ |
| bhbP Q88IC5 | ✓ | ✓ | ✗ |
| hbdH Q88IC6 | ✓ | ✓ | ✗ |
| OXCT1 P55809 | ✓ | ✓ | ✗ |
| BktB (PSEPK candidate) Q88GH0 | ✗ | — | — |
A membrane permease imports D-3-hydroxybutyrate when the substrate is supplied extracellularly; intracellular ketone-body pathways do not require this part.
Supplies extracellular D-3-hydroxybutyrate to the catabolic reactions.
Oxidizes D-3-hydroxybutyrate to acetoacetate.
Ketone-body consumers can activate acetoacetate by CoA transfer from succinyl-CoA or by ATP-dependent ligation of free coenzyme A.
CoA-transferase implementation characteristic of animal ketolysis.
ATP-dependent bacterial acetoacetate-activation route.
Cleaves activated acetoacetate to two acetyl-CoA molecules.