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Literature summary for 3.4.24.18 extracted from

  • Hengst, J.A.; Bond, J.S.
    Transport of meprin subunits through the secretory pathway: role of the transmembrane and cytoplasmic domains and oligomerization (2004), J. Biol. Chem., 279, 34856-34864.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information replacement of enzyme transmembrane and cytoplasmic domains, alphaT and alphaC, with their beta counterparts allows rapid movement of the alpha subunit to the cell surface. Enzyme alphaT and alphaC domains substituted into mephrin beta delayed movement of this chimera through the secretory pathway. Enzyme mutant C320ADELTAI, lacking a 56 amino acid inserted domain and unable to form disulfide bridges or higher order oligomers, is transported through the secretory pathway, but more slowly than mephrin beta Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Mus musculus
-
-

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-