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L-Isoleucine

Names
IUPAC name Isoleucine
Other names 2-Amino-3-methylpentanoic acid
Identifiers
CAS Number	73-32-5
3D model (JSmol)	Interactive image
ChEBI	CHEBI:58045
ChemSpider	6067
DrugBank	DB00167
ECHA InfoCard	100.000.726
KEGG	D00065
PubChem CID	791
UNII	04Y7590D77
CompTox Dashboard (EPA)	DTXSID501096647 DTXSID1047441, DTXSID501096647
InChI InChI=1S/C6H13NO2/c1-3-4(2)5(7)6(8)9/h4-5H,3,7H2,1-2H3,(H,8,9)/t4-,5-/m0/s1Key: AGPKZVBTJJNPAG-WHFBIAKZSA-N InChI=1/C6H13NO2/c1-3-4(2)5(7)6(8)9/h4-5H,3,7H2,1-2H3,(H,8,9)/t4-,5-/m0/s1Key: AGPKZVBTJJNPAG-WHFBIAKZBB
SMILES CC(C)(C(=O)O)N
Properties
Chemical formula	C6H13NO2
Molar mass	131.175 g·mol
Supplementary data page
Isoleucine (data page)
Except where otherwise noted, data are given for materials in their standard state (at 25 °C , 100 kPa). Y verify (what is  ?) Infobox references

Isoleucine (abbreviated as ilu or I) is an α-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. However, isoleucine present in nature exists in one enantiomeric form, (2S,3S)-2-amino-3-methylpentanoic acid.

Biosynthesis

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, it is synthesized via several steps, starting from pyruvic acid and alpha-ketoglutarate. Enzymes involved in this biosynthesis include:

1. Acetolactate synthase (also known as acetohydroxy acid synthase)
2. Acetohydroxy acid isomeroreductase
3. Dihydroxyacid dehydratase
4. Valine aminotransferase

Catabolism

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.

Biotin, sometimes referred to as Vitamin B7 or Vitamin H, is an absolute requirement for the full catabolism of isoleucine (as well as leucine). Without adequate biotin, the human body will be unable to fully break down isoleucine and leucine molecules . This can lead to numerous physiological issues (related to muscle maintenance and protein synthesis, lipid metabolism, and fatty acid metabolism) as well as cognitive issues resulting from general metabolic pathway failure and the irritating effects of hydroxyisovalerate, a byproduct of incomplete isoleucine catabolism. Isovaleric acidemia is an example of a disorder caused by incomplete catabolism of leucine.

Nutritional Sources

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.

Isomers of isoleucine

L-isoleucine (2S,3S) and D-isoleucine (2R,3R)

L-allo-isoleucine (2S,3R) and D-allo-isoleucine (2R,3S)

Synthesis

Isoleucine can be synthesized in a multistep procedure starting from 2-bromobutane and diethylmalonate. Synthetic isoleucine was originally reported in 1905.

German chemist Felix Ehrlich discovered isoleucine in hemoglobin in 1903.

References

1. IUPAC-IUBMB Joint Commission on Biochemical Nomenclature. "Nomenclature and Symbolism for Amino Acids and Peptides". Recommendations on Organic & Biochemical Nomenclature, Symbols & Terminology etc. Retrieved 2007-05-17.
2. Nelson, D. L.; Cox, M. M. "Lehninger, Principles of Biochemistry" 3rd Ed. Worth Publishing: New York, 2000. ISBN 1-57259-153-6.
3. http://www.metametrix.com/learning-center/case-studies/2004/biotin-detoxification-needs-in-cognitively-delayed-adult
4. , List is in order of highest to lowest of per 200 Calorie serving of the food, not volume or weight.
5. "dl-Isoleucine". Organic Syntheses. 1955; Collected Volumes, vol. 3, p. 495.
6. Bouveault and Locquin, Compt. rend., 141, 115 (1905).

External links

• Food Sources of Isoleucine
• Isoleucine and valine biosynthesis

v t e Encoded (proteinogenic) amino acids
General topics	Protein Peptide Genetic code
By properties	Aliphatic Branched-chain amino acids (Valine Isoleucine Leucine) Methionine Alanine Proline Glycine Aromatic Histidine Tyrosine Tryptophan Phenylalanine Polar, uncharged Asparagine Glutamine Serine Threonine Positive charge (pKa) Lysine (≈10.8) Arginine (≈12.5) Histidine (≈6.1) Pyrrolysine Negative charge (pKa) Aspartic acid (≈3.9) Glutamic acid (≈4.1) Selenocysteine (≈5.4) Cysteine (≈8.3) Tyrosine (≈10.1)
Amino acids types: Encoded (proteins) Essential Non-proteinogenic Ketogenic Glucogenic Secondary amino Imino acids D-amino acids Dehydroamino acids

• Proteinogenic amino acids
• Glucogenic amino acids
• Ketogenic amino acids
• Branched-chain amino acids
• Essential amino acids