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BRENDA support

Literature summary for 1.6.2.2 extracted from

  • Colombo, S.; Longhi, R.; Alcaro, S.; Ortuso, F.; Sprocati, T.; Flora, A.; Borgese, N.
    N-myristoylation determines dual targeting of mammalian NADH-cytochrome b5 reductase to ER and mitochondrial outer membranes by a mechanism of kinetic partitioning (2005), J. Cell Biol., 168, 735-745.
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum protein lacking N-myristoylation Rattus norvegicus 5783
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mitochondrion N-myristoylation is required for correct targeting Rattus norvegicus 5739
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Organism

Organism UniProt Comment Textmining
Rattus norvegicus
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recombinant enzyme
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Posttranslational Modification

Posttranslational Modification Comment Organism
lipoprotein N-myristoylation is required for correct targeting to mitochondria. Part of the protein is targeted to the endoplasmic reticulum without myristoylation, which interferes with interaction of the nascent chain with signal recognition particle, while a portion is myristoylated and targeted to mitochondria Rattus norvegicus