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1.13.12.24: calcium-regulated photoprotein

This is an abbreviated version!
For detailed information about calcium-regulated photoprotein, go to the full flat file.

Word Map on EC 1.13.12.24

Reaction

[aequorin]
+ 3 Ca2+ =
[aequorin] 1,2-dioxetan-3-one

Synonyms

aequorin, alcium-activated photoprotein, berovin, BFP-aq, blue fluorescent protein, Ca2+-binding photoprotein, Ca2+-regulated photoprotein, clytin, halistaurin, mitrocomin, mnemiopsin, mnemiopsin 1, mnemiopsin 2, mnemiopsin1, obelin, phialidin

ECTree

     1 Oxidoreductases
         1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
             1.13.12 With incorporation of one atom of oxygen (internal monooxygenases or internal mixed-function oxidases)
                1.13.12.24 calcium-regulated photoprotein

Crystallization

Crystallization on EC 1.13.12.24 - calcium-regulated photoprotein

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method at 20°C, crystal structures of the apoAequorin complexes with the chiral deaza-analogs (S)-daCTZ and (S)-HM-daCTZ are determined, suggesting that the hydroxy moiety at the C6-hydroxyphenyl group and the carbonyl moiety of the imidazopyrazinone ring in coelenterazine are essential to bind the apoAequorin molecule through hydrogen bonding
to 1.7 A resolution. A calcium ion is observed in each of the three EF-hand loops that have the canonical calcium-binding sequence, and each is coordinated in the characteristic pentagonal bipyramidal configuration. The calcium-loaded apo-protein retains the same compact scaffold and overall fold as the unreacted photoprotein containing the bound substrate, 2-hydroperoxycoelenterazine
to 2.3 A resolution. Aequorin is a globular molecule containing a hydrophobic core cavity that accommodates the ligand coelenterazine-2-hydroperoxide
recombinantly expressed in Escherichia coli with Hexa-His-tag tail at N-terminal
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
to 1.7 A resolution. A calcium ion is observed in each of the three EF-hand loops that have the canonical calcium-binding sequence, and each is coordinated in the characteristic pentagonal bipyramidal configuration. The calcium-loaded apo-protein retains the same compact scaffold and overall fold as the unreacted photoprotein containing the bound substrate, 2-hydroperoxycoelenterazine and also the same as the Ca2+-discharged obelin bound with the product, coelenteramide