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Literature summary extracted from

  • Molakarimi, M.; Gorman, M.; Mohseni, A.; Pashandi, Z.; Taghdir, M.; Naderi-Manesh, H.; Sajedi, R.; Parker, M.
    Reaction mechanism of the bioluminescent protein mnemiopsin1 revealed by X-ray crystallography and QM/MM simulations (2019), J. Biol. Chem., 294, 20-27 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.12.24 expression in Escherichia coli BL21(DE3)Star cells Mnemiopsis leidyi

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.13.12.24 sitting drop vapor diffusion method, crystal structure of Cd2+-loaded apo-mnemiopsin1 at 2.15 A resolution. The structure reveals that mnemiopsin1 has a two-domain fold with four alpha-helices in each domain Mnemiopsis leidyi

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.13.12.24 24500
-
gel filtartion Mnemiopsis leidyi

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.12.24 [apoaequorin] + coelenterazine + O2 + 3 Ca2+ Mnemiopsis leidyi
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[excited state blue fluorescent protein] + CO2
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?

Organism

EC Number Organism UniProt Comment Textmining
1.13.12.24 Mnemiopsis leidyi E0WVU4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.12.24
-
Mnemiopsis leidyi

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.12.24 [apoaequorin] + coelenterazine + O2 + 3 Ca2+
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Mnemiopsis leidyi [excited state blue fluorescent protein] + CO2
-
?
1.13.12.24 [apoaequorin] + coelenterazine + O2 + 3 Ca2+ the reaction mechanism of the bioluminescent protein mnemiopsin1 is revealed by X-ray crystallography and QM/MM simulations. A water molecule in the coelenteramide binding cavity is identified that forms a hydrogen bond with the amide nitrogen atom of coelenteramide, which, in turn, is hydrogen-bonded via another water molecule to Tyr-131. This observation supports the hypothesis that the function of the coelenteramide-bound water molecule is to catalyze the 2-hydroperoxycoelenterazine decarboxylation reaction by protonation of a dioxetanone anion, thereby triggering the bioluminescence reaction Mnemiopsis leidyi [excited state blue fluorescent protein] + CO2
-
?

Synonyms

EC Number Synonyms Comment Organism
1.13.12.24 mnemiopsin1
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Mnemiopsis leidyi