Uox encodes mouse uricase/urate oxidase (EC 1.7.3.3), a uricase-family enzyme that oxidizes urate to 5-hydroxyisourate in the urate degradation branch of purine catabolism. UniProt describes the reaction as urate + oxygen + water producing 5-hydroxyisourate and hydrogen peroxide, and structural and evolutionary evidence supports a cofactor-independent urate oxidase reaction. The conserved primary cellular site is the peroxisome, with additional UniProt-cited evidence for a liver mitochondrial pool; the broader upstream nucleoside and nucleotide catabolic steps are carried out by other enzymes of purine catabolism, not by Uox itself.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0019628 urate catabolic process | IBA GO_REF:0000033 | ACCEPT | Summary: Uox participates in urate catabolism by catalyzing urate oxidation. Reason: Urate oxidation is an early step in urate degradation, consistent with Uox function. Supporting Evidence: PMID:16462750 two proteins encoded by mouse genes catalyze two consecutive steps following urate oxidation to 5-hydroxyisourate (HIU) file:mouse/Uox/Uox-uniprot.txt PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from urate: step 1/3. file:mouse/Uox/Uox-deep-research-falcon.md Falcon places Uox downstream of xanthine dehydrogenase/oxidase in mammalian purine catabolism, where peroxisomal Uox oxidizes urate to 5-hydroxyisourate. |
| GO:0006145 purine nucleobase catabolic process | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Uox contributes to purine nucleobase catabolism via the urate degradation step. Reason: Urate is a purine breakdown product; Uox acts downstream in this pathway but is not the sole purine catabolic enzyme. Supporting Evidence: PMID:16462750 two proteins encoded by mouse genes catalyze two consecutive steps following urate oxidation to 5-hydroxyisourate (HIU) file:mouse/Uox/Uox-deep-research-falcon.md Falcon describes Uox as the downstream urate oxidation step in purine catabolism rather than an enzyme acting throughout all purine nucleobase catabolic reactions. |
| GO:0005777 peroxisome | IBA GO_REF:0000033 | ACCEPT | Summary: Uox localizes to the peroxisomal compartment. Reason: Biochemical fractionation indicates urate oxidase is closely associated with peroxisomes. Supporting Evidence: PMID:3200253 fatty acyl-CoA oxidase and urate oxidase both of which were indicated as showing a closer association with the peroxisomal compartment file:mouse/Uox/Uox-uniprot.txt SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:23085393}. file:mouse/Uox/Uox-deep-research-falcon.md Falcon summarizes mammalian Uox as a peroxisomal hepatic uricase. |
| GO:0004846 urate oxidase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Uox catalyzes urate oxidation to 5-hydroxyisourate in the urate degradation pathway. Reason: Urate oxidation and uricase activity are described for mouse tissues, matching the specific enzymatic function of Uox. Supporting Evidence: PMID:16462750 two proteins encoded by mouse genes catalyze two consecutive steps following urate oxidation to 5-hydroxyisourate (HIU) PMID:4207016 Developmental changes of adenosine deaminase, xanthine oxidase, and uricase in mouse tissues. file:mouse/Uox/Uox-uniprot.txt Reaction=urate + O2 + H2O = 5-hydroxyisourate + H2O2; EC=1.7.3.3. file:mouse/Uox/Uox-deep-research-falcon.md Falcon describes Uox as a cofactor-independent urate oxidase that catalyzes oxidation of uric acid to 5-hydroxyisourate using molecular oxygen. |
| GO:0004846 urate oxidase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Uox catalyzes urate oxidation to 5-hydroxyisourate in the urate degradation pathway. Reason: Urate oxidation and uricase activity are described for mouse tissues, matching the specific enzymatic function of Uox. Supporting Evidence: PMID:16462750 two proteins encoded by mouse genes catalyze two consecutive steps following urate oxidation to 5-hydroxyisourate (HIU) PMID:4207016 Developmental changes of adenosine deaminase, xanthine oxidase, and uricase in mouse tissues. |
| GO:0005739 mitochondrion | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: UniProt reports a mouse liver mitochondrial pool of Uox, but the conserved and best-supported primary location for uricase is peroxisome. Reason: The UniProt subcellular-location mapping and Nakamura study support retaining the mitochondrial annotation, while Falcon and older fractionation work place the core urate oxidase function in peroxisomes. Supporting Evidence: file:mouse/Uox/Uox-uniprot.txt SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:23085393}. Mitochondrion {ECO:0000269|PubMed:23085393}. file:mouse/Uox/Uox-deep-research-falcon.md Falcon reports that in terrestrial vertebrates, including rodents, uricase resides in peroxisomes and forms a core peroxisomal crystalloid in hepatocytes. |
| GO:0005777 peroxisome | IEA GO_REF:0000044 | ACCEPT | Summary: Uox localizes to the peroxisomal compartment. Reason: Biochemical fractionation indicates urate oxidase is closely associated with peroxisomes. Supporting Evidence: PMID:3200253 fatty acyl-CoA oxidase and urate oxidase both of which were indicated as showing a closer association with the peroxisomal compartment |
| GO:0006144 purine nucleobase metabolic process | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Broad purine nucleobase metabolism term; Uox acts in urate degradation. Reason: Evidence supports urate oxidation within purine metabolism, but the term is broader than the direct reaction. Supporting Evidence: PMID:16462750 two proteins encoded by mouse genes catalyze two consecutive steps following urate oxidation to 5-hydroxyisourate (HIU) |
| GO:0016491 oxidoreductase activity | IEA GO_REF:0000043 | MODIFY | Summary: General oxidoreductase activity is correct but too broad for Uox. Reason: Evidence supports the specific urate oxidase activity rather than a generic oxidoreductase term. Proposed replacements: urate oxidase activity Supporting Evidence: PMID:16462750 two proteins encoded by mouse genes catalyze two consecutive steps following urate oxidation to 5-hydroxyisourate (HIU) |
| GO:0004846 urate oxidase activity | ISO GO_REF:0000096 | ACCEPT | Summary: Uox catalyzes urate oxidation to 5-hydroxyisourate in the urate degradation pathway. Reason: Urate oxidation and uricase activity are described for mouse tissues, matching the specific enzymatic function of Uox. Supporting Evidence: PMID:16462750 two proteins encoded by mouse genes catalyze two consecutive steps following urate oxidation to 5-hydroxyisourate (HIU) PMID:4207016 Developmental changes of adenosine deaminase, xanthine oxidase, and uricase in mouse tissues. |
| GO:0005777 peroxisome | ISO GO_REF:0000096 | ACCEPT | Summary: Uox localizes to the peroxisomal compartment. Reason: Biochemical fractionation indicates urate oxidase is closely associated with peroxisomes. Supporting Evidence: PMID:3200253 fatty acyl-CoA oxidase and urate oxidase both of which were indicated as showing a closer association with the peroxisomal compartment |
| GO:0019628 urate catabolic process | ISO GO_REF:0000096 | ACCEPT | Summary: Uox participates in urate catabolism by catalyzing urate oxidation. Reason: Urate oxidation is an early step in urate degradation, consistent with Uox function. Supporting Evidence: PMID:16462750 two proteins encoded by mouse genes catalyze two consecutive steps following urate oxidation to 5-hydroxyisourate (HIU) |
| GO:0019628 urate catabolic process | IEA GO_REF:0000120 | ACCEPT | Summary: Uox participates in urate catabolism by catalyzing urate oxidation. Reason: Urate oxidation is an early step in urate degradation, consistent with Uox function. Supporting Evidence: PMID:16462750 two proteins encoded by mouse genes catalyze two consecutive steps following urate oxidation to 5-hydroxyisourate (HIU) |
| GO:0004846 urate oxidase activity | IDA PMID:16462750 Completing the uric acid degradation pathway through phyloge... | ACCEPT | Summary: Uox catalyzes urate oxidation to 5-hydroxyisourate in the urate degradation pathway. Reason: Urate oxidation and uricase activity are described for mouse tissues, matching the specific enzymatic function of Uox. Supporting Evidence: PMID:16462750 two proteins encoded by mouse genes catalyze two consecutive steps following urate oxidation to 5-hydroxyisourate (HIU) PMID:4207016 Developmental changes of adenosine deaminase, xanthine oxidase, and uricase in mouse tissues. |
| GO:0006149 deoxyinosine catabolic process | IDA PMID:16462750 Completing the uric acid degradation pathway through phyloge... | MARK AS OVER ANNOTATED | Summary: Uox catalyzes urate oxidation and does not directly carry out upstream nucleoside catabolic steps. Reason: Pathway-membership annotation. MGI annotates Uox, Urah and Urad uniformly to the upstream purine-nucleoside and nucleotide catabolic terms from PMID:16462750, treating the urate-degradation steps as the tail of every purine catabolic pathway, and the cached record is abstract-only. Uox catalyses only the urate oxidation step, so the term covers upstream steps Uox does not catalyse, but an experimental annotation is not removed on the strength of an abstract (second-pass re-review changed REMOVE to MARK_AS_OVER_ANNOTATED). Supporting Evidence: PMID:16462750 two proteins encoded by mouse genes catalyze two consecutive steps following urate oxidation to 5-hydroxyisourate (HIU) |
| GO:0006157 deoxyadenosine catabolic process | IDA PMID:16462750 Completing the uric acid degradation pathway through phyloge... | MARK AS OVER ANNOTATED | Summary: Uox catalyzes urate oxidation and does not directly carry out upstream nucleoside catabolic steps. Reason: Pathway-membership annotation. MGI annotates Uox, Urah and Urad uniformly to the upstream purine-nucleoside and nucleotide catabolic terms from PMID:16462750, treating the urate-degradation steps as the tail of every purine catabolic pathway, and the cached record is abstract-only. Uox catalyses only the urate oxidation step, so the term covers upstream steps Uox does not catalyse, but an experimental annotation is not removed on the strength of an abstract (second-pass re-review changed REMOVE to MARK_AS_OVER_ANNOTATED). Supporting Evidence: PMID:16462750 two proteins encoded by mouse genes catalyze two consecutive steps following urate oxidation to 5-hydroxyisourate (HIU) |
| GO:0006161 deoxyguanosine catabolic process | IDA PMID:16462750 Completing the uric acid degradation pathway through phyloge... | MARK AS OVER ANNOTATED | Summary: Uox catalyzes urate oxidation and does not directly carry out upstream nucleoside catabolic steps. Reason: Pathway-membership annotation. MGI annotates Uox, Urah and Urad uniformly to the upstream purine-nucleoside and nucleotide catabolic terms from PMID:16462750, treating the urate-degradation steps as the tail of every purine catabolic pathway, and the cached record is abstract-only. Uox catalyses only the urate oxidation step, so the term covers upstream steps Uox does not catalyse, but an experimental annotation is not removed on the strength of an abstract (second-pass re-review changed REMOVE to MARK_AS_OVER_ANNOTATED). Supporting Evidence: PMID:16462750 two proteins encoded by mouse genes catalyze two consecutive steps following urate oxidation to 5-hydroxyisourate (HIU) |
| GO:0006147 guanine catabolic process | IDA PMID:16462750 Completing the uric acid degradation pathway through phyloge... | MARK AS OVER ANNOTATED | Summary: Uox catalyzes urate oxidation and does not directly carry out upstream nucleoside catabolic steps. Reason: Pathway-membership annotation. MGI annotates Uox, Urah and Urad uniformly to the upstream purine-nucleoside and nucleotide catabolic terms from PMID:16462750, treating the urate-degradation steps as the tail of every purine catabolic pathway, and the cached record is abstract-only. Uox catalyses only the urate oxidation step, so the term covers upstream steps Uox does not catalyse, but an experimental annotation is not removed on the strength of an abstract (second-pass re-review changed REMOVE to MARK_AS_OVER_ANNOTATED). Supporting Evidence: PMID:16462750 two proteins encoded by mouse genes catalyze two consecutive steps following urate oxidation to 5-hydroxyisourate (HIU) |
| GO:0009114 hypoxanthine catabolic process | IDA PMID:16462750 Completing the uric acid degradation pathway through phyloge... | MARK AS OVER ANNOTATED | Summary: Uox catalyzes urate oxidation and does not directly carry out upstream nucleoside catabolic steps. Reason: Pathway-membership annotation. MGI annotates Uox, Urah and Urad uniformly to the upstream purine-nucleoside and nucleotide catabolic terms from PMID:16462750, treating the urate-degradation steps as the tail of every purine catabolic pathway, and the cached record is abstract-only. Uox catalyses only the urate oxidation step, so the term covers upstream steps Uox does not catalyse, but an experimental annotation is not removed on the strength of an abstract (second-pass re-review changed REMOVE to MARK_AS_OVER_ANNOTATED). Supporting Evidence: PMID:16462750 two proteins encoded by mouse genes catalyze two consecutive steps following urate oxidation to 5-hydroxyisourate (HIU) |
| GO:0006148 inosine catabolic process | IDA PMID:16462750 Completing the uric acid degradation pathway through phyloge... | MARK AS OVER ANNOTATED | Summary: Uox catalyzes urate oxidation and does not directly carry out upstream nucleoside catabolic steps. Reason: Pathway-membership annotation. MGI annotates Uox, Urah and Urad uniformly to the upstream purine-nucleoside and nucleotide catabolic terms from PMID:16462750, treating the urate-degradation steps as the tail of every purine catabolic pathway, and the cached record is abstract-only. Uox catalyses only the urate oxidation step, so the term covers upstream steps Uox does not catalyse, but an experimental annotation is not removed on the strength of an abstract (second-pass re-review changed REMOVE to MARK_AS_OVER_ANNOTATED). Supporting Evidence: PMID:16462750 two proteins encoded by mouse genes catalyze two consecutive steps following urate oxidation to 5-hydroxyisourate (HIU) |
| GO:0006154 adenosine catabolic process | IDA PMID:16462750 Completing the uric acid degradation pathway through phyloge... | MARK AS OVER ANNOTATED | Summary: Uox catalyzes urate oxidation and does not directly carry out upstream nucleoside catabolic steps. Reason: Pathway-membership annotation. MGI annotates Uox, Urah and Urad uniformly to the upstream purine-nucleoside and nucleotide catabolic terms from PMID:16462750, treating the urate-degradation steps as the tail of every purine catabolic pathway, and the cached record is abstract-only. Uox catalyses only the urate oxidation step, so the term covers upstream steps Uox does not catalyse, but an experimental annotation is not removed on the strength of an abstract (second-pass re-review changed REMOVE to MARK_AS_OVER_ANNOTATED). Supporting Evidence: PMID:16462750 two proteins encoded by mouse genes catalyze two consecutive steps following urate oxidation to 5-hydroxyisourate (HIU) |
| GO:0004846 urate oxidase activity | IDA PMID:4207016 Developmental changes of adenosine deaminase, xanthine oxida... | ACCEPT | Summary: Uox catalyzes urate oxidation to 5-hydroxyisourate in the urate degradation pathway. Reason: Urate oxidation and uricase activity are described for mouse tissues, matching the specific enzymatic function of Uox. Supporting Evidence: PMID:16462750 two proteins encoded by mouse genes catalyze two consecutive steps following urate oxidation to 5-hydroxyisourate (HIU) PMID:4207016 Developmental changes of adenosine deaminase, xanthine oxidase, and uricase in mouse tissues. |
| GO:0009115 xanthine catabolic process | IDA PMID:4207016 Developmental changes of adenosine deaminase, xanthine oxida... | UNDECIDED | Summary: Cannot be adjudicated here: PMID:4207016 is cached abstract-only. Prior observation, not a verdict: Uox is uricase, not xanthine oxidase. Reason: PMID:4207016 is cached abstract-only, so the curator's experimental evidence cannot be inspected here; per CLAUDE.md an experimental annotation is not overruled on that basis. Recorded observation, not a verdict: The cited study distinguishes xanthine oxidase from uricase; Uox activity is specific to urate oxidation. Supporting Evidence: PMID:4207016 Developmental changes of adenosine deaminase, xanthine oxidase, and uricase in mouse tissues. |
| GO:0006204 IMP catabolic process | IDA PMID:16462750 Completing the uric acid degradation pathway through phyloge... | MARK AS OVER ANNOTATED | Summary: Uox catalyzes urate oxidation and does not directly carry out upstream nucleoside catabolic steps. Reason: Pathway-membership annotation. MGI annotates Uox, Urah and Urad uniformly to the upstream purine-nucleoside and nucleotide catabolic terms from PMID:16462750, treating the urate-degradation steps as the tail of every purine catabolic pathway, and the cached record is abstract-only. Uox catalyses only the urate oxidation step, so the term covers upstream steps Uox does not catalyse, but an experimental annotation is not removed on the strength of an abstract (second-pass re-review changed REMOVE to MARK_AS_OVER_ANNOTATED). Supporting Evidence: PMID:16462750 two proteins encoded by mouse genes catalyze two consecutive steps following urate oxidation to 5-hydroxyisourate (HIU) |
| GO:0046059 dAMP catabolic process | IDA PMID:16462750 Completing the uric acid degradation pathway through phyloge... | MARK AS OVER ANNOTATED | Summary: Uox catalyzes urate oxidation and does not directly carry out upstream nucleoside catabolic steps. Reason: Pathway-membership annotation. MGI annotates Uox, Urah and Urad uniformly to the upstream purine-nucleoside and nucleotide catabolic terms from PMID:16462750, treating the urate-degradation steps as the tail of every purine catabolic pathway, and the cached record is abstract-only. Uox catalyses only the urate oxidation step, so the term covers upstream steps Uox does not catalyse, but an experimental annotation is not removed on the strength of an abstract (second-pass re-review changed REMOVE to MARK_AS_OVER_ANNOTATED). Supporting Evidence: PMID:16462750 two proteins encoded by mouse genes catalyze two consecutive steps following urate oxidation to 5-hydroxyisourate (HIU) |
| GO:0005777 peroxisome | IDA PMID:16462750 Completing the uric acid degradation pathway through phyloge... | ACCEPT | Summary: Uox localizes to the peroxisomal compartment. Reason: Biochemical fractionation indicates urate oxidase is closely associated with peroxisomes. Supporting Evidence: PMID:3200253 fatty acyl-CoA oxidase and urate oxidase both of which were indicated as showing a closer association with the peroxisomal compartment |
| GO:0046038 GMP catabolic process | IDA PMID:16462750 Completing the uric acid degradation pathway through phyloge... | MARK AS OVER ANNOTATED | Summary: Uox catalyzes urate oxidation and does not directly carry out upstream nucleoside catabolic steps. Reason: Pathway-membership annotation. MGI annotates Uox, Urah and Urad uniformly to the upstream purine-nucleoside and nucleotide catabolic terms from PMID:16462750, treating the urate-degradation steps as the tail of every purine catabolic pathway, and the cached record is abstract-only. Uox catalyses only the urate oxidation step, so the term covers upstream steps Uox does not catalyse, but an experimental annotation is not removed on the strength of an abstract (second-pass re-review changed REMOVE to MARK_AS_OVER_ANNOTATED). Supporting Evidence: PMID:16462750 two proteins encoded by mouse genes catalyze two consecutive steps following urate oxidation to 5-hydroxyisourate (HIU) |
| GO:0005777 peroxisome | IDA PMID:3200253 On the compartmentalization of catalase, fatty acyl-CoA oxid... | ACCEPT | Summary: Uox localizes to the peroxisomal compartment. Reason: Biochemical fractionation indicates urate oxidase is closely associated with peroxisomes. Supporting Evidence: PMID:3200253 fatty acyl-CoA oxidase and urate oxidase both of which were indicated as showing a closer association with the peroxisomal compartment |
| GO:0006196 AMP catabolic process | IDA PMID:16462750 Completing the uric acid degradation pathway through phyloge... | MARK AS OVER ANNOTATED | Summary: Uox catalyzes urate oxidation and does not directly carry out upstream nucleoside catabolic steps. Reason: Pathway-membership annotation. MGI annotates Uox, Urah and Urad uniformly to the upstream purine-nucleoside and nucleotide catabolic terms from PMID:16462750, treating the urate-degradation steps as the tail of every purine catabolic pathway, and the cached record is abstract-only. Uox catalyses only the urate oxidation step, so the term covers upstream steps Uox does not catalyse, but an experimental annotation is not removed on the strength of an abstract (second-pass re-review changed REMOVE to MARK_AS_OVER_ANNOTATED). Supporting Evidence: PMID:16462750 two proteins encoded by mouse genes catalyze two consecutive steps following urate oxidation to 5-hydroxyisourate (HIU) |
| GO:0046055 dGMP catabolic process | IDA PMID:16462750 Completing the uric acid degradation pathway through phyloge... | MARK AS OVER ANNOTATED | Summary: Uox catalyzes urate oxidation and does not directly carry out upstream nucleoside catabolic steps. Reason: Pathway-membership annotation. MGI annotates Uox, Urah and Urad uniformly to the upstream purine-nucleoside and nucleotide catabolic terms from PMID:16462750, treating the urate-degradation steps as the tail of every purine catabolic pathway, and the cached record is abstract-only. Uox catalyses only the urate oxidation step, so the term covers upstream steps Uox does not catalyse, but an experimental annotation is not removed on the strength of an abstract (second-pass re-review changed REMOVE to MARK_AS_OVER_ANNOTATED). Supporting Evidence: PMID:16462750 two proteins encoded by mouse genes catalyze two consecutive steps following urate oxidation to 5-hydroxyisourate (HIU) |
| GO:0005829 cytosol | TAS Reactome:R-MMU-9033925 | MARK AS OVER ANNOTATED | Summary: Reactome notes Pex5l binding to Uox, but this does not establish cytosolic residence as a primary location. Reason: The evidence is interaction-based and does not specify stable cytosolic localization for Uox. Supporting Evidence: Reactome:R-MMU-9033925 Pex5l binds monomeric Acox1 and monomeric Uox in preference to dimeric Acox1 and tetrameric Uox (Freitas et al. 2015) |
| GO:0005739 mitochondrion | HDA PMID:14651853 Integrated analysis of protein composition, tissue diversity... | KEEP AS NON CORE | Summary: The original HDA record comes from a mitochondrial proteome survey; UniProt separately cites a mouse liver study supporting a mitochondrial Uox pool. Reason: Retain as non-core because mitochondrial Uox has some protein-level support, but it is not the conserved primary localization emphasized by uricase pathway and localization literature. Supporting Evidence: PMID:14651853 we performed a proteomic survey of mitochondria from mouse brain, heart, kidney, and liver file:mouse/Uox/Uox-uniprot.txt SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:23085393}. Mitochondrion {ECO:0000269|PubMed:23085393}. |
| GO:0005777 peroxisome | TAS PMID:11461119 Peroxisome proliferator-activated receptor alpha-responsive ... | ACCEPT | Summary: Uox localizes to the peroxisomal compartment. Reason: PMID:11461119 reports peroxisome proliferation-related expression; peroxisomal localization is supported by fractionation data. Supporting Evidence: PMID:3200253 fatty acyl-CoA oxidase and urate oxidase both of which were indicated as showing a closer association with the peroxisomal compartment |
| GO:0006144 purine nucleobase metabolic process | TAS PMID:11461119 Peroxisome proliferator-activated receptor alpha-responsive ... | KEEP AS NON CORE | Summary: Broad purine nucleobase metabolism term; Uox acts in urate degradation. Reason: PMID:11461119 is expression-focused; functional support comes from urate oxidation evidence. Supporting Evidence: PMID:16462750 two proteins encoded by mouse genes catalyze two consecutive steps following urate oxidation to 5-hydroxyisourate (HIU) |
| GO:0004846 urate oxidase activity | TAS PMID:11461119 Peroxisome proliferator-activated receptor alpha-responsive ... | ACCEPT | Summary: Uox catalyzes urate oxidation to 5-hydroxyisourate in the urate degradation pathway. Reason: PMID:11461119 reports expression changes; enzymatic activity is supported by other studies. Supporting Evidence: PMID:16462750 two proteins encoded by mouse genes catalyze two consecutive steps following urate oxidation to 5-hydroxyisourate (HIU) PMID:4207016 Developmental changes of adenosine deaminase, xanthine oxidase, and uricase in mouse tissues. |
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Download this section (compressed HTML)Q: What fraction of endogenous mouse liver Uox activity is mitochondrial under normal, fasted, or SIRT5-perturbed conditions, compared with the peroxisomal pool?
Suggested experts: urate metabolism biochemists, peroxisome and mitochondrial proteomics experts
Q: Should the MGI annotations to specific upstream nucleoside, nucleotide, and xanthine catabolic processes be retired or replaced by urate catabolic process for Uox?
Suggested experts: GO biological process curators, mouse genome annotation curators
Experiment: Quantitatively fractionate mouse liver peroxisomes, mitochondria, and cytosol under fed and fasted conditions, measuring endogenous Uox protein, peroxisomal and mitochondrial marker purity, and urate oxidase activity in each fraction.
Hypothesis: Most endogenous Uox activity resides in peroxisomes, with any mitochondrial pool representing a smaller and condition-dependent non-core localization.
Type: Endogenous localization and activity fractionation
Experiment: In Uox-null and rescued mouse hepatocytes, trace labeled urate, xanthine, inosine, and AMP into 5-hydroxyisourate/allantoin-pathway products while assaying xanthine oxidase separately.
Hypothesis: Uox loss specifically blocks urate-to-5-hydroxyisourate conversion and does not directly impair upstream nucleoside, nucleotide, or xanthine catabolic reactions except through pathway accumulation.
Type: Purine pathway specificity curation assay
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