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Coelenterazine information


Coelenterazine
Names
IUPAC name
6-(4-Hydroxyphenyl)-2-[(4-hydroxyphenyl)methyl]-8-(phenylmethyl)-7H-imidazo[1,2-a]pyrazin-3-one
Other names
Renilla luciferin
Identifiers
CAS Number
  • 55779-48-1 checkY
3D model (JSmol)
  • Interactive image
ChEBI
  • CHEBI:2311 checkY
ChemSpider
  • 2728 checkY
ECHA InfoCard 100.164.960 Edit this at Wikidata
PubChem CID
  • 135445694
UNII
  • 3O1CB88RRD checkY
CompTox Dashboard (EPA)
  • DTXSID80204342 Edit this at Wikidata
InChI
  • InChI=1S/C26H21N3O3/c30-20-10-6-18(7-11-20)15-23-26(32)29-16-24(19-8-12-21(31)13-9-19)27-22(25(29)28-23)14-17-4-2-1-3-5-17/h1-13,16,27,30-31H,14-15H2 checkY
    Key: YHIPILPTUVMWQT-UHFFFAOYSA-N checkY
  • InChI=1S/C26H21N3O3/c30-20-10-6-18(7-11-20)15-23-26(32)29-16-24(19-8-12-21(31)13-9-19)27-22(25(29)28-23)14-17-4-2-1-3-5-17/h1-13,16,27,30-31H,14-15H2
SMILES
  • C1=CC=C(C=C1)CC2=C3N=C(C(=O)N3C=C(N2)C4=CC=C(C=C4)O)CC5=CC=C(C=C5)O
Properties
Chemical formula
C26H21N3O3
Molar mass 423.472 g·mol−1
Appearance Orange-yellow crystals
Melting point 175 to 178 °C (347 to 352 °F; 448 to 451 K)
Absorbance ε435 = 9800 M−1 cm−1 (methanol)[1]
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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Infobox references

Coelenterazine is a luciferin, a molecule that emits light after reaction with oxygen, found in many aquatic organisms across eight phyla.[1] It is the substrate of many luciferases such as Renilla reniformis luciferase (Rluc), Gaussia luciferase (Gluc), and photoproteins, including aequorin, and obelin. All these proteins catalyze the oxidation of this substance, a reaction catalogued EC 1.13.12.5.

  1. ^ a b Shimomura, O. (2006). Bioluminescence: Chemical Principles and Methods. World Scientific Publishing. pp. 159–65. ISBN 978-981-256-801-4.

and 24 Related for: Coelenterazine information

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Coelenterazine

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Coelenterazine is a luciferin, a molecule that emits light after reaction with oxygen, found in many aquatic organisms across eight phyla. It is the substrate...

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Aequorin

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prosthetic group coelenterazine, the luciferin. This is to say, apoaequorin is the enzyme produced in the photocytes of the animal, and coelenterazine is the substrate...

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Luciferin

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mononucleotide and a fatty aldehyde found in bioluminescent bacteria. Coelenterazine is found in radiolarians, ctenophores, cnidarians, squid, brittle stars...

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Bioluminescence

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triphosphate (ATP). In evolution, luciferins vary little: one in particular, coelenterazine, is found in 11 different animal phyla, though in some of these, the...

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Luciferase

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fluorescent protein (GFP). Calcium triggers release of the luciferin (coelenterazine) from the luciferin binding protein. The substrate is then available...

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Coelenteramine

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metabolic product of the bioluminescent reactions in organisms that utilize coelenterazine. It was first isolated from Aequorea victoria along with coelenteramide...

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Eukrohnia fowleri

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bioluminescence that is thought to be coelenterazine based. While both species use luciferases in conjunction with coelenterazine for light emission, the luciferase...

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Conchoecia

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Conchoeciinae. The genus contains bioluminescent species. Conchoecia have a coelenterazine luciferin based bioluminescent system, unlike the cypridinid luciferin...

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Halocyprididae

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as Conchoecia pseudodiscophora, which are believed to use coelenterazine and a coelenterazine luciferase rather than vargulin. The following genera are...

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Aequorea macrodactyla

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apoaequorin, the luminophore coelenterazine, and molecular oxygen. These proteins function together. As calcium binds to coelenterazine, (a bioluminescent molecule...

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Aequorea victoria

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Johnson isolated the protein aequorin, and its small molecule cofactor, coelenterazine, from large numbers of Aequorea jellyfish at Friday Harbor Laboratories...

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Pyrosoma atlanticum

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(RLuc). Further study of the luciferase showed that it reacted with coelenterazine to produce light, much like RLuc. Five specimens of the penaeid shrimp...

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Splendid lanternshark

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that contain coelenterazine, a manner of obtaining coelenterazine found in other bioluminescent species. Continued detection of coelenterazine and the related...

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Caecosagitta

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macrocephala has a secreted bioluminescence that is thought to be coelenterazine based. The luciferase is highly unstable, being unable to survive a...

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Coelenteramide

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of the bioluminescent reactions in many marine organisms that use coelenterazine. It was first isolated as a blue fluorescent protein from Aequorea victoria...

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Assay

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reporter assays using i.e. Luciferase, calcium signaling assays using Coelenterazine, CFSE or Calcein Immunostaining of cells on slides by Microscopy (ImmunoHistoChemistry...

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Stomiiformes

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glandular organs is the product of an enzymatic reaction, a catylization of coelenterazine by calcium ions.[citation needed] During the day, Stomiiformes stay...

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Calcium imaging

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on aequorin and the luciferin coelenterazine. Ca2+ binding causes a conformational change that facilitates coelenterazine oxidation. The resultant photoproduct...

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Bioluminescence imaging

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Sea pansy) requires its substrate, coelenterazine, to be injected as well. As opposed to luciferin, coelenterazine has a lower bioavailability (likely...

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EF hand

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binding component apoaequorin (AQ) and the chemiluminescent molecule coelenterazine. The AQ portion of this protein contains the EF-hand calcium binding...

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Kamo Aquarium

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"if you mix coelenterazine with food, it will shine in two weeks." Then, with the introduction of Shimomura, he took over coelenterazine from Katsunori...

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Bioreporter

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jellyfish Aequorea victoria. Upon addition of calcium ions (Ca2+) and coelenterazine, a reaction occurs whose result is the generation of blue light in the...

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Vargulin

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525 nm filter). The vargulin does not cross react with luciferases using coelenterazine or Firefly luciferin. Vargulin (with the associated luciferase) has...

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Slendertail lanternshark

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luciferase activity. The reaction to create light in this enzyme is based on coelenterazine and happens without any assistance of a symbiotic relationship with...

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