Biochemical Effects in Animals
Stephen P. Coburn in The Chemistry and Metabolism of 4′-Deoxypyridoxine, 2018
Bergamini et al.47 administered 20 mg deoxypyridoxine per day intraperitoneally for 30 days to rabbits apparently receiving a normal B6 diet. Two-dimensional paper chromatography of serum revealed that in controls, the major spots were alanine, valine, and leucine-phenylalanine. After treatment with deoxypyridoxine, the concentrations tyrosine, lysine, and arginine seemed to increase. Threonine was markedly increased in three of the four animals examined. Methionine was detected in three of the four treated animals but in neither of the two controls. Proline and serine seemed to be reduced. Aspartic acid, glutamic acid, glycine, tryptophan, alanine, valine, leucine, phenylalanine, and histidine were unchanged. Similar trends were found in the animals receiving deoxypyridoxine plus cholesterol. This differs from the results of Matano301 who reported that injection of normal mice with deoxypyridoxine produced an increase in glutamic acid, alanine, glycine, and valine in the cerebral cortex.
Threonine
Linda M. Castell, Samantha J. Stear (Nottingham), Louise M. Burke in Nutritional Supplements in Sport, Exercise and Health, 2015
Threonine is a nutritionally essential amino acid that has no metabolic precursor and thus must be obtained through the diet. Dietary threonine requirements for healthy adults are 15mg∙kg-1∙d-1. Foods that contain high amounts of threonine are cottage cheese, fish, chicken, sesame seeds and lentils. Relative to other amino acids, threonine is a major component of the protein core in the intestinal mucous. Animal studies show that manipulating dietary threonine intake can affect whole body and skeletal muscle protein metabolism. Specifically, low intakes of threonine have been demonstrated to reduce skeletal muscle and splanchnic tissue protein synthesis rates (Wang et al., 2007). As such, chronically consuming low intakes of dietary threonine, or any other essential amino acid, will impair tissue growth and function. Moreover, it has been shown that threonine supplementation has a positive effect upon immune function in pigs, mice and poultry (Defa et al., 1999; Li et al., 2007).
Methods for Sequence Determination
Roger L. Lundblad in Chemical Reagents for Protein Modification, 2020
Smithies et al.64 recommend hydrolysis of the thiazolinones or PTHs in 57% hydriodic acid (HI) at 127°C for 20 h. PTH-alanine, -serine, -carboxymethylcysteine, or -cysteine all hydrolyze to alanine. Threonine is identified as a-aminobutyric acid. PTH-tryptophan gives glycine plus alanine, and methionine is destroyed. Alkaline hydrolysis in 0.2 M NaOH plus 0.1 M sodium dithionite allows recovery of methionine and tryptophan and differentiation of alanine from serine or cysteine.
Study on the acute toxicity of sodium taurocholate via zebrafish mortality, behavioral response, and NMR-metabolomics analysis
Published in Drug and Chemical Toxicology, 2023
Isah Abdulazeez, Intan Safinar Ismail, Siti Munirah Mohd Faudzi, Annie Christianus, Seok-Giok Chong
Acute systemic inflammatory response syndrome has been reported to always induce a hypercatabolic condition leading to increased energy needs and protein catabolism (Johnson 2005). In this study, protein hyper-catabolism led to the downregulation of some amino acids. The significantly affected amino acids in the NaT-induced zebrafish as depicted in Figure 10, are downregulated homoserine, threonine, and glycine, and upregulated taurine and creatine. The production of essential amino acids, including threonine, methionine, and isoleucine, is mediated by homoserine. Threonine which is derived from homoserine acts in sustaining intestinal homeostasis by maintaining intestinal morphology, bacteria, the intestinal barrier, and immunological function. Threonine is employed to control immune cell differentiation, cytokine expression, and immune-related signaling cascades, such as mitogen-activated protein kinase (MAPK), the target of rapamycin (TOR), to preserve intestinal health when the intestinal tract is inflamed (Habte-Tsion et al. 2015, Gaifem et al. 2018). Threonine has been crucial in the growth and improves the protein synthesis of skeletal muscle in a variety of aquatic species and livestock (Wang et al. 2007; Hong et al. 2015). In epithelial tissues, such as mucins, threonine is necessary for the synthesis of threonine-rich proteins (Tang et al. 2021). The body uses dietary threonine for protein synthesis or oxidation to obtain energy. Since threonine is synthesized from homoserine, cellular consumption of these two amino acids should offset the negative effect of NaT.
Amino acids profiles of children who stutter compared to their fluent sibling
Published in International Journal of Psychiatry in Clinical Practice, 2020
Mazin Alqhazo, Ayat Bani Rashaid
Threonine is an essential amino acid which is important for regulating protein stability in the body. Because threonine is highly concentrated in the central nervous system, there has been interest in the use of this amino acid in the treatment of amyotrophic lateral sclerosis (Blin et al. 1992; Tandan et al. 1996). Amyotrophic lateral sclerosis is motor neuron disease characterised by stiff muscles and muscle twitching that leads to difficulty in speaking, swallowing, and breathing (Zarei et al. 2015). This amino acid was also included in the treatment of Multiple Sclerosis, including a reduction in spasticity (Hauser et al. 1992). Multiple sclerosis is a disruption of the myelin that covers the nerve cells resulting in a range of symptoms including physical and mental problems such as muscle spasms and difficulty in speech and swallowing (Compston and Coles 2008). Many studies have also found that threonine can help to control depression and can improve mental health (Chalexka-Franaszek and Chuang 1999; Beaulieu 2011). These symptoms associated with deficiency in threonine, could explain the physical and psychological behaviours associated with stuttering such as muscle tension and depression.
Design, synthesis and antifungal activity of threoninamide carbamate derivatives via pharmacophore model
Published in Journal of Enzyme Inhibition and Medicinal Chemistry, 2020
Xiu-Jiang Du, Xing-Jie Peng, Rui-Qi Zhao, Wei-Guang Zhao, Wei-Li Dong, Xing-Hai Liu
The three representative compounds (dimethomorph, iprovalicarb and mandipropamid) were performed using MOE. The 3D structures of the compounds were built by using the Builder option and geometry-optimized by using MMFF94x Forcefield and calculate forcefield partial charges. The three compounds were used successively for energy minimisation until the gradient value was smaller than 0.001 kcal/mol. The lowest-energy conformations of the three compounds were generated and the conformation of dimethomorph was served as templates in the study. Then the three compounds were aligned. The results are shown in Figure 1(b). Through three sub-types of molecular alignment, we built a pharmacophore model using SYBYL 6.9, which is shown in Figure 1(c). The results evaluated using pharmacophore scores. Threonine is an essential amino acid, which cannot be synthesised in humans. It’s structure is similar to valine. So a set of three threonine derivatives were designed and prepared using the above-described procedure for test case.