threonine

L-Threonine
IUPAC name	(2S,3R)-2-Amino-3-hydroxybutanoic acid
Identifiers
CAS number	[72-19-5]
PubChem	6288
EC number	200-774-1
SMILES	C[C@@H](O)[C@H](N)C(O)=O
Properties
Molecular formula	C4H9NO3
Molar mass	119.12 g mol−1
Supplementary data page
Structure and properties	n, εr, etc.
Thermodynamic data	Phase behaviour Solid, liquid, gas
Spectral data	UV, IR, NMR, MS
Except where noted otherwise, data are given for materials in their standard state (at 25 °C, 100 kPa) Infobox references

Threonine (abbreviated as Thr or T)^[1] is an α-amino acid with the chemical formula HO₂CCH(NH₂)CH(OH)CH₃. Its codons are ACU, ACA, ACC, and ACG. This essential amino acid is classified as polar. Together with serine and tyrosine, threonine is one of three proteinogenic amino acids bearing an alcohol group.

The threonine residue is susceptible to numerous posttranslational modifications. The hydroxy side chain can undergo O-linked glycosylation. In addition, threonine residues undergo phosphorylation through the action of a threonine kinase. In its phosphorylated form, it can be referred to as phosphothreonine.

Allo-threonine

With two chiral centers, threonine can exist in four possible stereoisomers, or two possible diastereomers of L-threonine. However, the name L-threonine is used for one single enantiomer, (2S,3R)-2-amino-3-hydroxybutanoic acid. The second diastereomer (2S,3S), which is rarely present in nature, is called L-allo-threonine.

Biosynthesis

As an essential amino acid, threonine is not synthesized in humans, hence we must ingest threonine in the form of threonine-containing proteins. In plants and microorganisms, threonine is synthesized from aspartic acid via α-aspartyl-semialdehyde and homoserine. Homoserine undergoes O-phosphorylation; this phosphate ester undergoes hydrolysis concomitant with relocation of the OH group.^[2] Enzymes involved in a typical biosynthesis of threonine include:

1. aspartokinase
2. α-aspartate semialdehyde dehydrogenase
3. homoserine dehydrogenase
4. homoserine kinase
5. threonine synthase.

Threonine biosynthesis

Metabolism

Threonine is metabolized in two ways:

• It is converted to pyruvate via threonine dehydrogenase. An intermediate in this pathway can undergo thiolysis with CoA to produce acetyl-CoA and glycine.
• In humans, it is converted to alpha-ketobutyrate in a less common pathway via the enzyme serine dehydratase, and thereby enters the pathway leading to succinyl-CoA.

Sources

Foods high in threonine include cottage cheese, poultry, fish, meat, lentils, and sesame seeds.^{[citation needed]}

Racemic threonine can be prepared from crotonic acid by alpha-functionalization using mercury(II) acetate.^[3]

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. http://www.chem.qmul.ac.uk/iupac/AminoAcid/. Retrieved on 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. ^ Carter, H. E.; West, H. D. (1955). "dl-Threonine". Org. Synth.; Coll. Vol. 3: 813. 

See also

• H.E. Carter, in collaboration with William C. Rose, first determined the structure of threonine.
• Harold Dadford West, the American biochemist who first synthesised threonine.

External links

• Threonine biosynthesis
• Computational Chemistry Wiki
• CID 205
• CID 6288