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1.13.12.5: Renilla-type luciferase

This is an abbreviated version!
For detailed information about Renilla-type luciferase, go to the full flat file.

Word Map on EC 1.13.12.5

Reaction

coelenterazine h
+
O2
=
coelenterazine h dioxetanone

Synonyms

19kOLase, aequorin, aequorin-1, BFP-aq, blue fluorescent protein from the calcium-binding photoprotein aequorin, Caussia princeps luciferase, clytin, extGLuc, extRLuc, firefly luciferase, fluc, Gaussia luciferase, Gaussia luciferase enzyme, Gaussia princeps luciferase, Gaussia-luciferase, GFP-aq, GLase, GLuc, Luc, luciferase, luciferase (Renilla luciferin), m-Rluc8, membrane-anchored RLUc, Oplophorus luciferase, PI-Rluc, R-Luc, Renilla luciferase, Renilla luciferase-547, Renilla luciferin 2-monooxygenase, Renilla muelleri luciferase, Renilla reniformis luciferase, Renilla-luciferase, Renilla-luciferin 2-monooxygenase, Renilla-type luciferase, RLase, RLase-547, RLuc, RLuc8, short peptide-inserted-Renilla luciferase

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)
                1.13.12.5 Renilla-type luciferase

Crystallization

Crystallization on EC 1.13.12.5 - Renilla-type luciferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
microbatch method is used for crystallization. The crystals of Ca2+-loaded apoaequorin are grown from 0.02 M CaCl2, 30% v/v 2-methyl-2,4-pentanediol, and 0.1 M sodium acetate (pH 4.6) during less than 1 week of incubation at 4°C. The maximum size of crystals is 0.35 * 0.3 * 0.25 mm
solution structure of fully active, recombinant GLuc. GLuc is an all-alphahelix protein made of nine helices. Two homologous sequential repeats form two anti-parallel bundles made by 4 helices and tied together by three disulfide bonds. The N-terminal helix 1 is grabbed by these 4 helices
free enzyme and in complex with coelenterazine,and mutant K25A/E277A. Diffraction to 1.4 A. Structures demonstrate a classic alpha/beta-hydrolase fold. The presumptive catalytic triad residues are D120, E144, and H285. Additionally determination of structure of the accessory green fluorescent protein
molecular docking simulations with the coelenterazine substrate. Two triads of residues are critical for catalysis. Putative catalytic triad residues D120, E144, and H285 bear only limited resemblance to those of aequorin. Residues N53, W121, and P220 are also involved in catalysis