Technical Information Amino Acids Glycine

Glycine

Glycine, denoted by the symbol Gly or G, is an amino acid characterized by a single hydrogen atom as its side chain. It is the simplest amino acid that remains stable. Glycine plays a crucial role in the formation of alpha-helices in secondary protein structures due to its compact structure. Consequently, it is the most abundant amino acid found in collagen triple-helices. Furthermore, glycine functions as an inhibitory neurotransmitter, and disruption of its release in the spinal cord, such as during a Clostridium tetani infection, can result in spastic paralysis due to uncontrolled muscle contractions. Notably, glycine is the only proteinogenic amino acid that lacks chirality, meaning it is achiral. Its minimal side chain, consisting of just one hydrogen atom, allows it to adapt to hydrophilic or hydrophobic environments. The primary role of glycine is to serve as a precursor for protein synthesis. While most proteins incorporate only small amounts of glycine, collagen stands as an exception with approximately 35% glycine content. This high proportion is attributed to the periodic repetition of glycine's involvement in collagen's helical structure formation in conjunction with hydroxyproline. Glycine is encoded by all codons that begin with GG (GGU, GGC, GGA, GGG).

Structure
CAS Number 56-40-6
Classification

Polar amino acids, including

Cysteine

Glycine

Glutamine

Threonine

Tyrosine

Serine

Asparagine
Categories
Glycine Cleavage Related Compounds
56-40-6 Glycine
[H-protein]-lipoyllysine
[H-protein]-S-aminomethyldihydrolipoyllysine
124-38-9 CO2
135-16-0 Tetrahydrofolate
[H-protein]-dihydrolipoyllysine
3432-99-3 5,10-Methylenetetrahydrofolate
7664-41-7 Ammonia

Glycine and Derivatives:

Glycine:

Derivatives: