As an essential amino acid, isoleucine is not synthesized in animals, hence it must be ingested, usually as a component of proteins. In plants and microorganisms, Isoleucine is synthesized via several steps, starting from pyruvic acid and alpha-ketoglutarate. Enzymes involved in this biosynthesis include:
Acetolactate synthase (also known as acetohydroxy acid synthase)
Acetohydroxy acid isomeroreductase
Isoleucine is both a glucogenic and a ketogenic amino acid. After transamination with alpha-ketoglutarate the carbon skeleton can be converted into either Succinyl CoA, and fed into the TCA cycle for oxidation or conversion into oxaloacetate for gluconeogenesis (hence glucogenic). It can also be converted into Acetyl CoA and fed into the TCA cycle by condensing with oxaloacetate to form citrate. In mammals Acetyl CoA cannot be converted back to carbohydrate but can be used in the synthesis of ketone bodies or fatty acids, hence ketogenic.
Even though this amino acid is not produced in animals, it is stored in high quantities. Foods that have high amounts of isoleucine include eggs, soy protein, seaweed, turkey, chicken, lamb, cheese, and fish.
Isoleucine (abbreviated as Ile or I) is an a-amino acid with the chemical formula HO2CCH(NH2)CH(CH3)CH2CH3. It is an essential amino acid, which means that humans cannot synthesize it, so it must be ingested. Its codons are AUU, AUC and AUA.
With a hydrocarbon side chain, isoleucine is classified as a hydrophobic amino acid. Together with threonine, isoleucine is one of two common amino acids that have a chiral side chain. Four stereoisomers of isoleucine are possible, including two possible diastereomers of L-isoleucine. Still, isoleucine present in nature exists in one enantiomeric form, (2S,3S)-2-amino-3-methylpentanoic acid.