UniProtKB entry for mouse Gulo/L-gulonolactone oxidase
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Gulo oxidizes L-gulono-1,4-lactone in the terminal step of L-ascorbate biosynthesis.
"Oxidizes L-gulono-1,4-lactone to hydrogen peroxide and L- xylo-hexulonolactone which spontaneously isomerizes to L-ascorbate."
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Gulo uses FAD as a cofactor.
"Name=FAD; Xref=ChEBI:CHEBI:57692"
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Gulo is an ER/microsomal single-pass membrane protein.
"Microsome membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}."
Falcon deep research report for mouse Gulo
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Falcon summarizes Gulo as an FAD-dependent ER/microsomal aldonolactone oxidoreductase in the terminal step of ascorbate biosynthesis.
"Enzyme: L‑gulonolactone oxidase (EC 1.1.3.8), terminal ascorbate biosynthesis step: L‑gulono‑1,4‑lactone + O2 → L‑ascorbate + H2O2; FAD‑dependent AlOR enzyme with N‑terminal FAD‑binding region and C‑terminal HWXK motif; integral ER/microsomal membrane protein with luminally oriented active site; predominant tissue locus in mammalian liver"
Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automated transfer of experimentally-verified manual GO annotation data to mouse-rat orthologs
Combined Automated Annotation using Multiple IEA Methods
Different induction of gulonolactone oxidase in aromatic hydrocarbon-responsive or -unresponsive mouse strains.
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Mouse liver microsomes produce ascorbate from gulonolactone.
"The mRNA level of gulonolactone oxidase and the microsomal ascorbate production from p-nitrophenyl glucuronide, D-glucuronic acid or gulonolactone in the liver of Ah-responsive and Ah-unresponsive mice were compared."
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AhR-responsive mice have higher and inducible Gulo expression and microsomal ascorbate production.
"In Ah-responsive mice, these parameters were higher originally, and they further increased upon in vivo addition of 3-methylcholanthrene, while in Ah-unresponsive mice the treatment was not effective."
Aortic wall damage in mice unable to synthesize ascorbic acid.
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Inactivation of Gulo makes mice dependent on dietary vitamin C.
"By inactivating the gene for L-gulono-gamma-lactone oxidase, a key enzyme in ascorbic acid synthesis, we have generated mice that, like humans, depend on dietary vitamin C."
Functional rescue of vitamin C synthesis deficiency in human cells using adenoviral-based expression of murine l-gulono-gamma-lactone oxidase.
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Murine Gulo cDNA encodes a functional FAD-containing enzyme.
"Cells infected with Gulo-expressing vectors overexpressed an FAD-containing protein that corresponded in size to that predicted for recombinant GULO protein and expressed a functional enzyme as measured by the conversion of l-gulono-gamma-lactone to ascorbic acid in cell-free extracts."
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Gulo transcript is highly expressed in mouse liver.
"Northern blot analysis revealed high expression of Gulo transcript in the liver."
Ascorbate synthesis pathway: dual role of ascorbate in bone homeostasis.
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This paper focuses on upstream D-glucuronate-to-L-gulonate enzymes in the mouse ascorbate synthesis pathway rather than directly assaying Gulo.
"Using mouse gene knock-out models, we identify aldehyde reductase (EC 1.1.1.2, Akr1a4 (GR)) and aldose reductase (EC 1.1.1.21, Akr1b3 (AR)) as the enzymes responsible for conversion of D-glucuronate to L-gulonate, a key step in the ascorbate (ASC) synthesis pathway in mice."