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Ligand [apoaequorin]

Basic Ligand Information

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (1 result)

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Show Natural Substrate (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.12.24

[apoaequorin] + coelenterazine + O2 + 3 Ca2+ = [excited state blue fluorescent protein] + CO2

765521, 765058

-

Substrate in Enzyme-catalyzed Reactions (7 results)

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Show Substrate (7 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.12.24

[apoaequorin] + coelenterazine + O2 + 3 Ca2+ = [excited state blue fluorescent protein] + CO2

765521, 744216, 765058, 764863, 765527

-

1.13.12.24

[apoaequorin] + coelenterazine + O2 = [aequorin] 1,2-dioxetan-3-one

744479

-

1.13.12.24

[apoaequorin] + coelenterazine + O2 = [apoaequorin] + coelenteramide + CO2 + hnu

744887

-

1.13.12.24

[apoaequorin] + cp-coelenterazine + O2 + 3 Ca2+ = [excited state blue fluorescent protein] + CO2

744216

-

1.13.12.24

[apoaequorin] + f-coelenterazine + O2 + 3 Ca2+ = [excited state blue fluorescent protein] + CO2

744216

-

1.13.12.24

[apoaequorin] + h-coelenterazine + O2 + 3 Ca2+ = [excited state blue fluorescent protein] + CO2

744216

-

1.13.12.24

[apoaequorin] + hcp-coelenterazine + O2 + 3 Ca2+ = [excited state blue fluorescent protein] + CO2

744216

-

1.13.12.24

7 entries

Product in Enzyme-catalyzed Reactions (1 result)

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Show Product (1 entry)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.12.24

[apoaequorin] + coelenterazine + O2 = [apoaequorin] + coelenteramide + CO2 + hnu

0

-

Enzyme Kinetic Parameters

References & Links

Literature References (7)

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Show Reference (7 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

744216

17254548

Imidazole-assisted catalysis of luminescence reaction in blue fluorescent protein from the photoprotein aequorin

2007

Inouye, S.; Sasaki, S.

Biochem. Biophys. Res. Commun.

354

650-655

744479

19362849

Selective protein modification by the hydroperoxide intermediate in a photoprotein, aequorin

2009

Doi, I.; Kuse, M.; Nishikawa, T.; Isobe, M.

Bioorg. Med. Chem.

17

3399-3404

744887

8462695

Bioluminescence of the Ca(2+)-binding photoprotein, aequorin, after histidine modification

1993

Ohmiya, Y.; Tsuji, F.I.

FEBS Lett.

320

267-270

764863

29382580

Bioluminescence and kinetic aspects of double mutated aequorin variants

2018

Zeinoddini, M.; Fathi-Roudsari, M.; Hosseinkhani, S.; Khajeh, K.

Int. J. Biol. Macromol.

112

163-168

765058

30420427

Reaction mechanism of the bioluminescent protein mnemiopsin1 revealed by X-ray crystallography and QM/MM simulations

2019

Molakarimi, M.; Gorman, M.; Mohseni, A.; Pashandi, Z.; Taghdir, M.; Naderi-Manesh, H.; Sajedi, R.; Parker, M.

J. Biol. Chem.

294

20-27

765521

34727376

Specific activities of hydromedusan Ca2+-regulated photoproteins

2022

Malikova, N.P.; Eremeeva, E.V.; Gulnov, D.V.; Natashin, P.V.; Nemtseva, E.V.; Vysotski, E.S.

Photochem. Photobiol.

98

275-283

765527

32057065

The interaction of C-terminal Tyr208 and Tyr13 of the first ?-helix ensures a closed conformation of ctenophore photoprotein berovin

2020

Burakova, L.P.; Eremeeva, E.V.; Vysotski, E.S.

Photochem. Photobiol. Sci.

19

313-323

Links to other databases for [apoaequorin]

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Show Links (1 entry)