82650-07-5

Usage

Uses

Used in Animal Nutrition:
L-Threonine hydrochloride is used as a nutritional supplement in animal feed to promote healthy growth in livestock. It supports the immune system and maintains proper muscle function, contributing to the overall well-being of animals.
Used in Pharmaceutical Industry:
L-Threonine hydrochloride is used as an active pharmaceutical ingredient in the development of various medications. Its stability and solubility properties make it suitable for formulation in different dosage forms.
Used in Chemical and Food Additive Production:
L-Threonine hydrochloride is utilized in the production of chemicals and food additives, enhancing the quality and functionality of these products.
Used in Cosmetics and Personal Care Products:
L-Threonine hydrochloride is used as an ingredient in the development of cosmetics and personal care products, providing benefits such as skin hydration and improving the texture of hair and nails.

InChI:InChI=1/C4H9NO3.ClH/c1-2(6)3(5)4(7)8;/h2-3,6H,5H2,1H3,(H,7,8);1H/t2?,3-;/m0./s1

Upstream product

• 1447695-69-3 cycloforskamide 
• 1207348-80-8 micropeptin MZ₇₇₁ 
• 1207348-78-4 micropeptin MZ₁₀₁₉ 
• 1207348-76-2 micropeptin MZ₉₃₉B 
• 1207348-74-0 micropeptin MZ₉₂₅ 
• 1207348-72-8 micropeptin MZ₉₃₉A 
• 1207348-70-6 micropeptin MZ₈₅₉ 
• 914606-75-0 micropeptin MZ₈₄₅ 
• 1383580-56-0 (2S,4S)-N-((6R,9R,12S,15S,16R,Z)-3-ethylidene-6-(4-hydroxybenzyl)-12-isobutyl-9-isopropyl-16-methyl-2,5,8,11,14-pentaoxo-1-oxa-4,7,10,13-tetraazacyclohexadecan-15-yl)-2,4-dimethylheptanamide 

Downstream Products

• 39994-75-7 H-DL-aThr-OMe*HCl 
• 39994-75-7 (+/-) threonine methyl ester hydrochloride 
• 72-19-5 L-threonine 
• 60538-17-2 (4S,5R)-4-methyl-2-phenyl-4,5-dihydrooxazole-4-carboxylic acid methyl ester 
• 33209-01-7 L-threonine amide hydrochloride 
• 80110-55-0 Boc-Tyr-Thr-OH 

Relevant academic research and scientific papers

Cycloforskamide, a cytotoxic macrocyclic peptide from the sea slug Pleurobranchus forskalii

A macrocylic dodecapeptide, cycloforskamide, was isolated from the sea slug Pleurobranchus forskalii, collected off Ishigaki Island, Japan. Its planar structure was deduced by extensive NMR analyses and was further confirmed by MS/MS fragmentation analyses. Finally, the absolute configuration was determined by total hydrolysis and chiral-phase gas chromatographic analysis. This novel dodecapeptide contains three d-amino acids and three thiazoline heterocycles and exhibits cytotoxicity against murine leukemia P388 cells, with an IC 50 of 5.8 μM.

Tumescenamide C, an antimicrobial cyclic lipodepsipeptide from Streptomyces sp.

Tumescenamide C, a new cyclic lipodepsipeptide, was isolated from a culture broth of an actinomycete Streptomyces sp. KUSC-F05. Tumescenamide C was a congener of tumescenamides A and B, representing a sixteen-membered ring system, consisting of two proteinogenic and three non-proteinogenic amino acids, to which a methyl-branched fatty acid was attached. The planar structure was determined by spectroscopic analysis, while its absolute stereochemistry was determined by chemical degradation and asymmetric synthesis. Tumescenamide C exhibited antimicrobial activity with high selectivity against Streptomyces species.

Micropeptins from an Israeli fishpond water bloom of the cyanobacterium microcystis sp

Seven new natural products, micropeptin MZ845 (1), micropeptin MZ859 (2), micropeptin MZ939A (3), micropeptin MZ925 (4), micropeptin MZ939B (5), micropeptin MZ1019 (6), and micropeptin MZ771 (7), as well as two known micropeptins, cyanopeptolin S (8) and cyanopeptolin SS (9), were isolated from the hydrophilic extract of the cyanobacterium Microcystis sp. that was collected from a fishpond in Kibbutz Ma'ayan Tzvi, Israel, in July 2006. The structures of the pure natural products were elucidated using spectroscopic methods, including UV, 1D and 2D NMR, and MS techniques. The absolute configuration of the chiral centers of the compounds was determined using Marfey's method for HPLC. The inhibitory activity of the compounds was determined for the serine proteases: trypsin, chymotrypsin, thrombin, and elastase. These micropeptins inhibited trypsin with IC50's that varied between 0.6 and 24.2 μM. The SAR of these micropeptins is discussed.