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Literature summary extracted from

  • Burakova, L.P.; Eremeeva, E.V.; Vysotski, E.S.
    The interaction of C-terminal Tyr208 and Tyr13 of the first ?-helix ensures a closed conformation of ctenophore photoprotein berovin (2020), Photochem. Photobiol. Sci., 19, 313-323 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.12.24 expression in Escherichia coli BL21-Gold (DE3) Codon Plus Beroe abyssicola

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.12.24 Ca2+ Ca2+-regulated photoprotein Beroe abyssicola

Organism

EC Number Organism UniProt Comment Textmining
1.13.12.24 Beroe abyssicola H8ZZK1
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.12.24
-
 Beroe abyssicola

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.12.24 [apoaequorin] + coelenterazine + O2 + 3 Ca2+ the interaction between C-terminal Tyr208 and Tyr13 of the berovin first alpha-helix is essential for the stabilization and proper orientation of the 2-hydroperoxy adduct of coelenterazine within the internal cavity as well as for supporting its closed conformation. In contrast to hydromedusan photoproteins, in berovin the interplay between Tyr residues is conditioned rather by the pi-pi interaction of their phenyl rings than by the formation of hydrogen bonds between OH-groups Beroe abyssicola [excited state blue fluorescent protein] + CO2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.13.12.24 berovin
-
 Beroe abyssicola

General Information

EC Number General Information Comment Organism
1.13.12.24 physiological function the enzyme is responsible for the bioluminescence of the ctenophore Beroe abyssicola Beroe abyssicola