Limelight

Limelight (also known as Drummond light or calcium light) is a type of stage lighting once used in theatres and music halls. An intense illumination is created when an oxyhydrogen flame is directed at a cylinder of quicklime (calcium oxide), which can be heated to 2,572 °C (4,662 °F) before melting. The light is produced by a combination of incandescence and candoluminescence. Although it has long since been replaced by electric lighting, the term has nonetheless survived, as someone in the public eye is still said to be “in the limelight.” The actual lights are called limes, a term which has been transferred to electrical equivalents.

History

The limelight effect was discovered in the 1820s by Goldsworthy Gurney, based on his work with the "oxy-hydrogen blowpipe," credit for which is normally given to Robert Hare. In 1825, a Scottish engineer, Thomas Drummond (1797–1840), saw a demonstration of the effect by Michael Faraday and realized that the light would be useful for surveying. Drummond built a working version in 1826, and the device is sometimes called the Drummond Light after him.

Limelight (disambiguation)

Limelight is a type of stage lighting used during the 1860s. It may also refer to:

Places

Film and TV

Music

Albums

Limelight (Belfast)

Limelight in Belfast, Northern Ireland is mid-sized live music and night club venue complex, which initially opened in 1987. The complex on the city's Ormeau Avenue consists of Limelight 1 & Limelight 2, as well as a bar called Katy's Bar. The outdoor terrace is called The Rock Garden.

Limelight has strong associations with new bands, homegrown talent, and indie/rock/metal club nights.

History

Limelight nightclub and adjoining Dome bar were first opened in 1987 by Patrick Lennon who had previously owned the Harp Bar based in Hill Street, Belfast. Growing over the years it eventually took over the adjoining building which was a premises owned by a spring and airbrake business (hence the "Spring and Airbrake" venue name).

In 2010 then owners, CDC Leisure, went into administration. In late 2011, the Limelight complex was purchased by Irish live music promoters MCD & Shine Productions. In late 2012 following a major refurbishment, the individual bars were rebranded, with the Spring and Airbrake being renamed to Limelight 1, Katy Daly's becoming Katy's Bar and the original Limelight venue becoming known as Limelight 2.

TYRP1

Tyrosinase-related protein 1, also known as TYRP1, is an enzyme which in humans is encoded by the TYRP1 gene.

Function

Tyrp1 is a melanocyte-specific gene product involved in melanin synthesis. While mouse Tyrp1 possesses dihydroxyindole carboxylic acid oxidase activity, the function in human melanocytes is less clear. In addition to its role in melanin synthesis, Tyrp1 is involved in stabilizing of tyrosinase protein and modulating its catalytic activity. Tyrp1 is also involved in maintenance of melanosome structure and affects melanocyte proliferation and melanocyte cell death.

Clinical significance

Mutations in the mouse Tyrp1 gene are associated with brown pelage and in the human TYRP1 gene with oculocutaneous albinism type 3 (OCA3). An allele of TYRP1 common in Solomon Islanders results in blond hair. Although the phenotype is similar to Northern European blond hair, this allele is not found in Europeans.

Regulation

The expression of TYRP1 is regulated by the microphthalmia-associated transcription factor (MITF).

Phosphoribosylanthranilate isomerase

In enzymology, a phosphoribosylanthranilate isomerase (EC 5.3.1.24) is an enzyme that catalyzes the third step of the synthesis of the amino acid tryptophan.

This enzyme participates in the phenylalanine, tyrosine and tryptophan biosynthesis pathway, also known as the aromatic amino acid biosynthesis pathway

In yeast it is encoded by the TRP1 gene.

Reaction

In other words, this enzyme has one substrate, N-(5-phospho-beta-D-ribosyl)anthranilate, and one product, 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. As the name phosphoribosylanthranilate isomerase suggests, it functions as an isomerase, rearranging the parts of the molecule without adding or removing molecules or atoms

Nomenclature

This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is N-(5-phospho-beta-D-ribosyl)anthranilate aldose-ketose-isomerase. Other names in common use include: