Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniPathway vocabulary mapping.
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
The identification of an integral membrane, cytochrome c urate oxidase completes the catalytic repertoire of a therapeutic enzyme.
Catalysis and Structure of Zebrafish Urate Oxidase Provide Insights into the Origin of Hyperuricemia in Hominoids.
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Zebrafish Uox was cloned and biochemically/structurally characterized as urate oxidase.
"A cDNA encoding the complete sequence of zebrafish urate oxidase"
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Zebrafish Uox catalyzes hydroxylation of urate to 5-hydroxyisourate, the first and rate-limiting step of the three-step uricolysis pathway converting urate to (S)-allantoin.
"Urate oxidase (uricase, Uox) catalyses hydroxylation of urate to give 5-hydroxyisourate (HIU)"
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Uricolysis is a conserved three-step pathway yielding the more soluble (S)-allantoin, with Uox catalyzing the first and rate-limiting step.
"This is the first and rate-limiting step of uricolysis, a three-step enzymatic pathway present in both prokaryotes and eukaryotes that converts urate into the more soluble (S)-allantoin"
A Trivalent Enzymatic System for Uricolytic Therapy of HPRT Deficiency and Lesch-Nyhan Disease.
Uricase-Deficient Larval Zebrafish with Elevated Urate Levels Demonstrate Suppressed Acute Inflammatory Response to Monosodium Urate Crystals and Prolonged Crystal Persistence.
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uox-deficient zebrafish larvae show elevated urate, supporting the in vivo urate-metabolism role.
"elevated urate levels at early larval stages"
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A zebrafish uox null mutant has elevated urate, a suppressed acute inflammatory response to MSU crystals, and prolonged in vivo crystal persistence, directly linking Uox function to urate handling and crystal-driven inflammation.
"describe a zebrafish uox null mutant that possesses elevated urate levels at"
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uox is expressed primarily in the developing liver at 2 dpf by whole-mount in situ hybridization, consistent with the liver as the principal site of larval uricolysis.
"in situ hybridization (WMISH) showed expression at 2 dpf in the developing liver, with weaker diffuse expression in the head and along the horizontal myoseptum (Figure 2A)"
UniProtKB entry Q6DG85 for Danio rerio uox
Falcon (Edison Scientific Literature) deep research report for Danio rerio uox (Q6DG85)
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Falcon synthesizes that zebrafish Uox is a classical cofactorless urate oxidase catalyzing oxidation/hydroxylation of urate to 5-hydroxyisourate (HIU).
"Zebrafish Uox catalyzes **oxidation/hydroxylation of urate to HIU**, and is described as the **classical cofactorless Uox** (i.e., it does not require a tightly bound organic cofactor)."
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Falcon places Uox among peroxisomal oxidases that use molecular oxygen as electron acceptor and generate hydrogen peroxide as a byproduct.
"Uox is grouped among peroxisomal oxidases that use **molecular oxygen (O₂)** as electron acceptor and generate **hydrogen peroxide (H₂O₂)** as a byproduct of oxidation chemistry"
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Falcon assigns Uox the first, rate-limiting step of the three-step uricolysis pathway, followed by Urah (HIU hydrolase) and Urad (OHCU decarboxylase) to (S)-allantoin.
"the canonical uricolysis pathway is a **three-enzyme** sequence in which Uox generates **5-hydroxyisourate (HIU)**, followed by HIU hydrolase (Urah) and OHCU decarboxylase (Urad) to yield **(S)-allantoin**."
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Falcon supports peroxisomal matrix localization of Uox via a C-terminal PTS1 (ARM) targeting signal and a zebrafish peroxisomal proteome inventory.
"DrUox encodes a C-terminal **ARM** tripeptide corresponding to a **PTS1** motif, indicating peroxisomal matrix import."
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Falcon reports the kinetic parameters of recombinant wild-type DrUox (Km ~11 uM, kcat ~4 per s) consistent with the UniProt KM value.
"**Wild-type DrUox:** **Km = 11 ± 1 μM**, **kcat ≈ 4 s⁻¹**."
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Falcon notes the homotetrameric T-fold architecture of zebrafish Uox with active sites at subunit interfaces.
"Zebrafish Uox forms a **tetramer** with the **T-fold** architecture typical of classical uricases; the functional active sites occur at subunit interfaces."