Égly

Égly is a commune in the Essonne department in Île-de-France in northern France.

Inhabitants of Égly are known as Aglatiens.

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Glycine

Glycine (abbreviated as Gly or G) is the smallest of the 20 amino acids commonly found in proteins, and indeed is the smallest possible (having a hydrogen substituent as its side-chain). The formula is NH₂CH₂COOH. Its codons are GGU, GGC, GGA, GGG of the genetic code.

Glycine is a colourless, sweet-tasting crystalline solid. It is unique among the proteinogenic amino acids in that it is achiral. It can fit into hydrophilic or hydrophobic environments , due to its minimal side chain of only one hydrogen atom.

History and etymology

Glycine was first isolated from gelatin in 1820. The name comes from the ancient Greek word γλυκύς "sweet tasting".

Production

Glycine was discovered in 1820, by Henri Braconnot who boiled a gelatinous object with sulfuric acid.

Glycine is manufactured industrially by treating chloroacetic acid with ammonia:

About 15 million kg are produced annually in this way.

In the USA (by GEO Specialty Chemicals, Inc.) and in Japan (by Showa Denko KK), glycine is produced via the Strecker amino acid synthesis.

L-allo-threonine aldolase

L-allo-threonine aldolase (GLY1, EC 4.1.2.49) is an enzyme catalyzing the conversion between L-allo-threonine (unusual stereoisomer) on one side and glycine plus acetaldehyde on another side. Artificial disabling (knockout) of this enzyme in wild bacteria has no significant effect. However such disabling suppresses the growth of mutants that already lack other enzyme, serine hydroxymethyltransferase. Hence L-allo-threonine aldolase provides the alternative pathway for cellular glycine when serine hydroxymethyltransferase is inert.E.coli L-allo-threonine aldolase is a highly termostable enzyme (survives 60 degrees C), this can be used for purification.

The enzyme is specific for L-allo-threonine and can not act on the more common L-threonine. It is different from EC 4.1.2.5 (L-threonine aldolase) and EC 4.1.2.48 (less specific enzyme that acts on both L-threonine and L-allo-threonine). A previously listed enzyme with highly similar name (allothreonine aldolase, past EC 4.1.2.6), was deleted in 1971 after it was found to be identical to EC 2.1.2.1.