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Literature summary for 1.16.3.1 extracted from

  • Lang, M.; Braun, C.L.; Kanost, M.R.; Gorman, M.J.
    Multicopper oxidase-1 is a ferroxidase essential for iron homeostasis in Drosophila melanogaster (2012), Proc. Natl. Acad. Sci. USA, 109, 13337-13342.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinantly expressed in Sf9 cells using the baculovirus expression system. Recombinant MCO1 is expressed without the von Willebrand factor domains and transmembrane segment, and Arg454 is mutated to alanine to reduce proteolytic cleavage Drosophila melanogaster

Protein Variants

Protein Variants Comment Organism
R454A Arg454 is mutated to Ala in order to reduce proteolytic cleavage Drosophila melanogaster

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster
-
-
-

Purification (Commentary)

Purification (Comment) Organism
using concanavalin-A-Sepharose and Q-sepharose Drosophila melanogaster

Source Tissue

Source Tissue Comment Organism Textmining
malpighian tubule
-
Drosophila melanogaster
-
midgut basal surface of midgut Drosophila melanogaster
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
MCO1 has ferroxidase activity Drosophila melanogaster

Synonyms

Synonyms Comment Organism
MCO1
-
Drosophila melanogaster
multicopper oxidase-1
-
Drosophila melanogaster

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Drosophila melanogaster

pH Range

pH Minimum pH Maximum Comment Organism
6 8 highest activity Drosophila melanogaster

General Information

General Information Comment Organism
malfunction knockdown of MCO1 is correlated with increased longevity on high-iron food and decreased iron accumulation Drosophila melanogaster