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Literature summary for 1.13.12.24 extracted from

  • Ohashi, W.; Inouye, S.; Yamazaki, T.; Hirota, H.
    NMR analysis of the Mg2+-binding properties of aequorin, a Ca2+-binding photoprotein (2005), J. Biochem., 138, 613-620 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Aequorea victoria

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ binding of Mg2+ to aequorin prevents the molecule from aggregating and stabilizes it in the monomeric form. Mg2+ binding induces conformational in the EF-hand loops. There are two Mg2+-binding sites, EF-hands I and III. EF-hand III binds to Mg2+ with higher affinity than EF-hand I, and only EF-hand III seems to be occupied by Mg2+ under physiological conditions Aequorea victoria

Organism

Organism UniProt Comment Textmining
Aequorea victoria P02592
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