3938-83-8

Usage

Uses

Used in Pharmaceutical Applications:
L-threonine is used as a pharmaceutical ingredient for promoting proper growth and immune function. It is essential for the body's ability to produce collagen and elastin, which are vital for healthy skin, hair, and nails.
Used in Nutritional Supplements:
L-threonine is used as a nutritional supplement to support overall health and well-being. It can be found in various dietary sources, including eggs, dairy products, certain meats, leafy green vegetables, nuts, and seeds, making it an important component of a balanced and healthy diet.
Used in the Central Nervous System:
L-threonine is used as a precursor for the synthesis of glycine, an inhibitory neurotransmitter in the central nervous system. This application helps maintain proper neurological function and supports the overall health of the brain and nervous system.
Used in the Food Industry:
L-threonine is used in the food industry as a natural additive to enhance the nutritional value of various products. It can be added to dietary supplements, protein powders, and other health products to support the body's amino acid requirements and promote overall health.
Used in Cosmetics:
L-threonine is used in the cosmetics industry for its role in promoting healthy skin, hair, and nails. It can be found in various skincare and hair care products, contributing to their nourishing and protective properties.
Used in Research and Development:
L-threonine is used in research and development for its potential applications in various fields, including pharmaceuticals, nutrition, and cosmetics. Its role in protein synthesis, immune function, and neurotransmitter production makes it a valuable compound for scientific study and innovation.

Upstream product

• 57229-74-0 (S)-2-hydroxysuccinamic acid 
• 56-12-2 4-amino-n-butyric acid 
• 40371-50-4 S-4-benzyloxycarbonylamino-2-hydroxybutyric acid 
• 1758-80-1 L-2,4-diaminobutyrate 
• 40732-91-0 γ-phthalimidoimino-α-hydroxybutyric acid 

Downstream Products

• 188753-46-0 (S)-2-Hydroxy-4-(5-methyl-2-nitro-phenylamino)-butyric acid 
• 207305-60-0 (S)-4-[(tert-butoxycarbonyl)amino]-2-hydroxybutanoic acid 
• 149137-92-8 (2S)-4-(p-nitrobenzyloxycarbonyl)-amino-2-hydroxybutyric acid 
• 48172-10-7 (+)-(2S)-4-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-2-hydroxybutanoic acid 
• 1455088-71-7 (S)-4-(1-cyano-4-hydroxy-7-phenoxyisoquinoline-3-carboxamido)-2-hydroxybutanoic acid 
• 1455086-97-1 2-(S)-hydroxy-4-[(4-hydroxy-7-phenoxyisoquinoline-3-carbonyl)amino]butyric acid 
• 1221492-53-0 N,N'-bis(benzyloxycarbonyl)-2-(S)-hydroxy-4-guanidino-butyric acid 
• 850397-64-7 4-Benzyloxycarbonylamino-2S-hydroxy butyric acid ethyl ester 
• 40371-50-4 S-4-benzyloxycarbonylamino-2-hydroxybutyric acid 
• 111607-75-1 (S)-hydroxy-3 phenylacetyl-1 pyrrolidinone-2 
• 34368-52-0 (S)-3-hydroxypyrrolidin-2-one 

Relevant academic research and scientific papers

α-Hydroxylation of Carboxylic Acids Catalyzed by Taurine Dioxygenase

Enzymes still have a limited application scope in synthetic organic chemistry. To expand this, different strategies exist that range from the de novo design of enzymes to the exploitation of the catalytic capabilities of known enzymes by converting different substrates; denoted as substrate promiscuity. We harnessed the synthetic potential offered by the taurine dioxygenase (TauD) from Escherichia coli (E. coli) by studying its promiscuous catalytic properties in the hydroxylation of carboxylic acid substrates. TauD showed high selectivities in the hydroxylation reaction but reduced levels of activity (26 % conversion, >96 % ee). We enhanced the enzyme substrate scope and improved the conversions for the tested substrates by introducing a point mutation at position 206 (F206Y). The conversions of the improved catalyst increased by at least 140 % compared to that of the wild-type enzyme. The number of carboxylic acids that accepted by the enzyme variant doubled from four to eight carboxylic acids.

Enantioselective Syntheses of (S)- and (R)-3-Hydroxypyrrolidin-2-ones via Lactate Dehydrogenase Catalysed Reductions of 4-Benzyloxycarbonylamino-2-oxobutanoic Acid

The first examples of the BS- and SE-lactate dehydrogenase catalysed reductions of an α-keto acid incorporating a nitrogen containing function in the side chain are described: (S)- and (R)-benzyloxycarbonylamino-2-hydroxybutanoic acids were prepared in good yield and excellent enantioselectivities and were converted to the (S)- and (R)-3-hydroxypyrrolidin-2-ones respectively.

Hydroxylations microbiologiques de pyrrolidinones-2 (note de laboratoire)

Microbial hydroxylations of various pyrrolidin-2 ones, especially N-acylated, with Beauveria sulfurescens have been carried out.The regioselectivity depends on the nature of the substituent on the nitrogen atom and the hydroxylation may occur at position 3,4 or 5 of the heterocycle.Hydroxylations at position 3 or 4 occur with low enantioselectivity.