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Literature summary for 2.4.1.222 extracted from

  • Serth, K.; Schuster-Gossler, K.; Kremmer, E.; Hansen, B.; Marohn-Köhn, B.; Gossler, A.
    O-Fucosylation of DLL3 is required for its function during somitogenesis (2015), PLoS ONE, 10, e0123776.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
coexpression of Flag-tagged DLL3 and HA-tagged LFNG in CHO cells, the two proteins coprecipitate Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
Golgi apparatus
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Mus musculus 5794
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trans-Golgi network
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Mus musculus 5802
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mus musculus the enzyme interacts with Delta-like 3 (DLL3), a member of the DSL family of Notch ligands, epidermal growth factor like repeats 2 and 5 of DLL3 are O-fucosylated at consensus sites for peptide-O-fucosyltransferase POFUT1, EC 2.4.1.221 ?
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?

Organism

Organism UniProt Comment Textmining
Mus musculus O09010 gene lfng
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme interacts with Delta-like 3 (DLL3), a member of the DSL family of Notch ligands, epidermal growth factor like repeats 2 and 5 of DLL3 are O-fucosylated at consensus sites for peptide-O-fucosyltransferase POFUT1, EC 2.4.1.221 Mus musculus ?
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?
additional information Delta-like 3 is O-fucosylated at epidermal growth factor repeats two and five, and the fucosylated protein is a substrate for FNG proteins in cultured cells, the O-fucose-linked residues in EGF 2 and/or 5 are elongated by fringe protein, enzyme LFNG. Recognition of DLL3 by LFNG also does not depend on the presence of O-linked fucose Mus musculus ?
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?

Synonyms

Synonyms Comment Organism
LFNG
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Mus musculus
Lunatic Fringe
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Mus musculus

General Information

General Information Comment Organism
malfunction loss of the DSL protein DLL3 in the mouse results in severe somite patterning defects, which are virtually indistinguishable from the defects in mice that lack the enzyme lunatic fringe. Embryos double homozygous for null mutations in Dll3 and Lfng are phenotypically indistinguishable from the single mutants supporting a potential common function. Mutation of the O-fucosylation sites in DLL3 does not disrupt the interaction of DLL3 with LFNG or full length Notch1or DLL1, and O-fucosylation-deficient DLL3 can still inhibit Notch in cis in vitro. In contrast to wild type DLL3, O-fucosylation-deficient DLL3 cannot compensate for the loss of endogenous DLL3 during somitogenesis in the embryo Mus musculus
physiological function enzyme lunatic fringe is a glycosyltransferase involved in modifying Notch signaling. modification of DLL3 by O-linked fucose via the action of enzyme lunatic fringe is essential for its function during somitogenesis Mus musculus