Literature summary for 1.13.12.24 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 .

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Cloned(Commentary)

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

Metals/Ions

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

Organism

Organism	UniProt	Comment	Textmining
Beroe abyssicola	H8ZZK1	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Beroe abyssicola

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
[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

Synonyms	Comment	Organism
berovin	-	Beroe abyssicola

General Information

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

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Release 2023.1 (January 2023)