Category
page 1Excitatory amino acids
DL-glutamic acid
amino acid and neurotransmitter
L-aspartic acid
chemical compound

L-Cysteine
thumb|Cysteine ball and stick model spinning
Cysteine (; symbol Cys or C) is a semiessential proteinogenic amino acid with the formula . The thiol side chain in cysteine enables the formation of disulfide bonds, and often participates in enzymatic reactions as a nucleophile. Cysteine is chiral, but both D and L-cysteine are found in nature. LCysteine is a protein monomer in all biota, and D-cysteine acts as a signaling molecule in mammalian nervous systems. Cysteine is named after its discovery in urine, which comes from the urinary bladder or cyst, from Greek κύστις kýstis, "bladder".

DL-proline
thumb|Proline ball and stick model spinning
Proline (symbol Pro or P) is an organic acid classed as a proteinogenic amino acid (used in the biosynthesis of proteins), although it does not contain the amino group but is rather a secondary amine. The secondary amine nitrogen is in the protonated form (NH2+) under biological conditions, while the carboxyl group is in the deprotonated −COO− form. The "side chain" from the α carbon connects to the nitrogen forming a pyrrolidine loop, classifying it as a aliphatic amino acid. It is non-essential in humans, meaning the body can synthesize it from the

DL-homocysteine
Homocysteine (; symbol Hcy) is a non-proteinogenic α-amino acid. It is a homologue of the amino acid cysteine, differing by an additional methylene bridge (). It is biosynthesized from methionine by the removal of its terminal Cε methyl group.