Need Assistance?

  • US & Canada:
  • UK: +
* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

L-Threonine is an essential amino acid found in high-protein foods.
Protein supplement in health care products.

L-Amino Acids
Catalog number
CAS number
Molecular Formula
Molecular Weight
(2S,3R)-2-amino-3-hydroxybutanoic acid
Threonine; H-Thr-OH; Threonin
White Solid
Melting Point
256°C (dec.)
Store at RT
Ingredient of health care products.
InChI Key
Canonical SMILES
1.Using the indicator amino acid oxidation technique to study threonine requirements in horses receiving a predominantly forage diet.
Mok CH;Levesque CL;Urschel KL J Anim Physiol Anim Nutr (Berl). 2018 Oct;102(5):1366-1381. doi: 10.1111/jpn.12927. Epub 2018 Jun 14.
Threonine has been reported to be the second limiting amino acid in typical equine diets, but its actual requirement has not been determined in horses. To evaluate amino acid metabolism and requirements, the indicator amino acid oxidation (IAAO) method has been successfully used in other species. The objective of this research was to estimate threonine requirements in mature horses fed timothy hay and concentrate in 4:1 ratio using the IAAO method. Six Thoroughbred mares (579.9 ± 46.7 kg) received each of 6 levels of threonine intake, 41, 51, 61, 70, 80 and 89 mg/kg BW/day, in a randomly determined order. Each study period was 7-day long, and on day 6, blood samples were collected before and 90 min after feeding to measure amino acid concentrations using HPLC. On day 7, horses underwent IAAO procedures, which included a 2-hr primed, constant intravenous infusion of [;13; C]sodium bicarbonate to measure total CO;2; production and a 4-hr primed, constant oral administration of [1-;13; C]phenylalanine to estimate phenylalanine oxidation to CO;2; . Blood and breath samples were collected to measure blood [;13; C]phenylalanine, using GC-MS analysis and breath ;13; CO;2; enrichment, using an infrared isotope analyser.
2.Inhibitors of Serine/Threonine Protein Phosphatases: Biochemical and Structural Studies Provide Insight for Further Development.
Swingle MR;Honkanen RE Curr Med Chem. 2018 May 7. doi: 10.2174/0929867325666180508095242. [Epub ahead of print]
BACKGROUND: ;The reversible phosphorylation of proteins regulates many key functions in eukaryotic cells. Phosphorylation is catalyzed by protein kinases, with the majority of phosphorylation occurring on side chains of serine and threonine residues. The phosphomonoesters generated by protein kinases are hydrolyzed by protein phosphatases. In the absence of a phosphatase the half-time for the hydrolysis of alkyl phosphate dianions at 25º C is over 1 trillion years; knon ~2 x 10-20 sec-1. Therefore, ser/thr phosphatases are critical for processes controlled by reversible phosphorylation.;METHODS: ;This review is based on a search of the literature in available databases. We compare the catalytic mechanism of PPP-family phosphatases (PPPases) and the interactions of inhibitors that target these enzymes.;RESULTS: ;PPPases are metal-dependent hydrolases that enhance the rate of hydrolysis ([kcat/kM]/knon ) by a factor of ~1021, placing them among the most powerful known catalysts on earth. Biochemical and structural studies indicate the remarkable catalytic proficiencies of PPPases are achieved by 10 conserved amino acids, DXH(X)~26DXXDR(X)~20-26NH(X)~50H(X)~25-45R(X)~30-40H. Six act as metal-coordinating residues.
3.Leptin regulates KATP channel trafficking in pancreatic β-cells by a signaling mechanism involving AMP-activated protein kinase (AMPK) and cAMP-dependent protein kinase (PKA).
Chen PC;Kryukova YN;Shyng SL J Biol Chem. 2013 Nov 22;288(47):34098-109. doi: 10.1074/jbc.M113.516880. Epub 2013 Oct 7.
Pancreatic β-cells secrete insulin in response to metabolic and hormonal signals to maintain glucose homeostasis. Insulin secretion is under the control of ATP-sensitive potassium (KATP) channels that play key roles in setting β-cell membrane potential. Leptin, a hormone secreted by adipocytes, inhibits insulin secretion by increasing KATP channel conductance in β-cells. We investigated the mechanism by which leptin increases KATP channel conductance. We show that leptin causes a transient increase in surface expression of KATP channels without affecting channel gating properties. This increase results primarily from increased channel trafficking to the plasma membrane rather than reduced endocytosis of surface channels. The effect of leptin on KATP channels is dependent on the protein kinases AMP-activated protein kinase (AMPK) and PKA. Activation of AMPK or PKA mimics and inhibition of AMPK or PKA abrogates the effect of leptin. Leptin activates AMPK directly by increasing AMPK phosphorylation at threonine 172. Activation of PKA leads to increased channel surface expression even in the presence of AMPK inhibitors, suggesting AMPK lies upstream of PKA in the leptin signaling pathway.

Online Inquiry

Verification code
Inquiry Basket