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... is an α-amino acid with the chemical formula HO2CCH(NH2)CH(OH)CH3. Foods high in threonine include cottage cheese, poultry, fish, meat, lentils, and sesame seeds.... |
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As an essential amino acid, threonine is not synthesized in humans, hence we must ingest threonine in the form of threonine-containing proteins....
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Threonine
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As an essential amino acid, threonine is not synthesized in humans, hence we must ingest threonine in the form of threonine-containing proteins....
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Threonine |
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As an essential amino acid, threonine is not synthesized in humans, hence we must ingest threonine in the form of threonine-containing proteins....
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Fish
Lentils
Meat- From an article in Wikipedia Mar 8, 2009
Threonine (abbreviated as Thr or T) 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.
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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.
Enzymes involved in a typical biosynthesis of threonine include:
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aspartokinase
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α-aspartate semialdehyde dehydrogenase
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homoserine dehydrogenase
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homoserine kinase
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threonine synthase.
No higher resolution available.
Thr_biosynthesis.gif (768 × 489 pixels, file size: 8 KB, MIME type: image/gif)
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.
Racemic threonine can be prepared from crotonic acid by alpha-functionalization using mercury(II) acetate.
**
Read The complete Article in Wikipedia, Mar 8, 2009
*Threonine. (2009, March 1). In Wikipedia, The Free Encyclopedia.
Retrieved 06:36, March 8, 2009, from
http://en.wikipedia.org/w/index.php?title=
Threonine&oldid=274239835
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Read the complete Article in Wikipedia June 23 2011
** Threonine. (2011, April 23). In Wikipedia, The Free Encyclopedia.
Retrieved 23:54, June 23, 2011, from
http://en.wikipedia.org/w/index.php?title=
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