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Single Amino Acids
Published in Luke R. Bucci, Nutrition Applied to Injury Rehabilitation and Sports Medicine, 2020
Proteins are composed of amino acids linked together into discrete chains. Peptides are short chains of amino acids (2 to 20 amino acid residues). Amino acids are the precursors and raw materials for proteins, peptides, nucleotides, and parts of phospholipids. Amino acid metabolism encompasses and directly impacts almost every aspect of cellular function. Pools of individual amino acids exist inside of cells, in plasma, and in other extracellular fluids. Amino acids are ubiquitous in the human body. This chapter will explore the use of individual amino acids for enhancement of musculoskeletal healing. The range of studies is from enhanced absorption of minerals to pharmacological pain control, illustrating the enormous breadth of functions for amino acids. One caveat must be considered about single amino acids, or, for that matter, any single nutrient. The human metabolism and the healing response is a complex, dynamic system with numerous homeostatic controls. Simply adding one ingredient to a complex system may or may not accentuate the desired result, or it may have unforeseen consequences. In other words, adding a single nutrient to metabolism and expecting it to exert measurable effects on the net outcome is an uphill climb. Nevertheless, with the widespread availability of pure, individual amino acids, a considerable literature has accumulated on the effects of single amino acids on musculoskeletal healing.
L-2-hydroxyglutaric aciduria
Published in William L. Nyhan, Georg F. Hoffmann, Aida I. Al-Aqeel, Bruce A. Barshop, Atlas of Inherited Metabolic Diseases, 2020
William L. Nyhan, Georg F. Hoffmann, Aida I. Al-Aqeel, Bruce A. Barshop
Independently, Topcu and colleagues [5] used a genome-wide scan for alterations in five consanguineous families. They localized the gene to 5.4 Mb on chromosome 14q22.1. In a narrowed area of ten genes, they found mutations in patients with the disease. They named the gene duranin after the author of the first paper on the disease [1]. Two Turkish families were homozygous for a mutation in exon 7 which led to P302L. In two others, a deletion at c1115 in exon 9 indicated a premature stop. In another, a transversion in intron 7 yielded aberrant splicing of exon 7. Mutations have also been reported by Vilarinho et al. [22], often leading to a premature stop codon, an altered reading frame, or modified splicing that would yield a truncated protein. Missense mutations changed strictly conserved or semiconserved amino acid residues with very different size or polarity. A multicenter study revealed mutations in this gene in 106 patients from 83 families [7].
The Modification of Lysine
Published in Roger L. Lundblad, Chemical Reagents for Protein Modification, 2020
On occasion, the modification of an amino acid residue in a protein is associated with an apparent increase in catalytic activity. This was the situation with the modification of 14S and 30S dynein adenosine triphosphatase activities with trinitrobenzenesulfonic acid.129 In this study, the reaction was performed in 0.030 M barbital, pH 8.5 at 25°C. The extent of modification was determined spectrophotometrically at 345 nm (∊ = 1.45 x 104M−1 cm−1). In studies similar to those obtained with glutamate dehydrogenase as discussed above,124 glutathione reductase was demonstrated to reduce trinitrobenzenesulfonate.130 Inhibition of glutathione reductase was noted at low concentration (0.05 μM) of trinitrobenzenesulfonate.
The role of N-myristoyltransferase 1 in tumour development
Published in Annals of Medicine, 2023
Hong Wang, Xin Xu, Jiayi Wang, Yongxia Qiao
Tumourigenesis is characterized by biological properties such as sustained proliferation, resistance to apoptosis, metastasis, epithelial mesenchymal transition, metabolic reprogramming and immune escape [1], and is caused by altered activity of intracellular signalling, metabolic and gene regulatory networks. Protein post-translational modifications are tightly associated with in these alterations [2–4]. Protein post-translational modifications are covalent attachments of specific motifs to amino acid residues of proteins under the catalytic action of enzymes. Typical post-translational modifications are methylation, phosphorylation, ubiquitination and lipidation [4]. In recent years, the importance of one of these lipid modifications, myristoylation, in the development of human tumourigenesis has emerged [5,6]. A series of studies has shown that myristoylation plays an essential role in signal transduction, protein stability and protein localization at the membrane [7].
Forecasting most deleterious nsSNPs in human TLR9 gene and their cumulative impact on biophysical features of the protein using in silico approaches
Published in Systems Biology in Reproductive Medicine, 2023
Heena Gautam, Ved Vrat Verma, Syed Akhtar Husain, Mausumi Bharadwaj
Looking into insight, an evolutionarily conserved amino acid profile of most deleterious nsSNPs provides essential information to understand the possible impact of deleterious nsSNPs on the structural and functional features of the protein. The ConSurf web server identifies whether the position of every individual amino acid is exposed on the protein surface or buried inside the core protein. The outcomes of the ConSurf web server revealed six deleterious nsSNPs (P139H, R257C, L283P, G514D, L544Q, and H566Y) as evolutionary conserved (Table 3 and Figure 2). However, the other two deleterious nsSNPs C265Y and W670R are predicted to be as moderately conserved (Table 3). The two variants (G514D and H566Y) are structurally exposed whereas the other six nsSNPS (P139H, R257C, L283P, L544Q, and W670R) are buried inside the core protein (Table 3). Evolutionarily, conserved amino acid residues are known to play a vital role in crucial structural and functional features of the protein. Therefore, it is argued that mutations at highly conserved sites have a direct impact on changes in the structural and functional features of TLR9.
Dyhidro-β-agarofurans natural and synthetic as acetylcholinesterase and COX inhibitors: interaction with the peripheral anionic site (AChE-PAS), and anti-inflammatory potentials
Published in Journal of Enzyme Inhibition and Medicinal Chemistry, 2022
Julio Alarcón-Enos, Evelyn Muñoz-Núñez, Margarita Gutiérrez, Soledad Quiroz-Carreño, Edgar Pastene-Navarrete, Carlos Céspedes Acuña
The rest of the compounds evaluated interact in a similar way with some of the amino acids that are part of the PAS. In addition, all of them, with the exception of compound 11, interact through π bonds with amino acids located in the gorge centre of the enzyme such as Phe 330, Trp 279, Phe 290 and Phe 331. These interactions are important because these amino acid residues connect the peripheral site and the anionic subsite in the active site of the enzyme. When inhibitor entering the enzymés active site, possibilities that substrate can reach the bottom of the gorge are limited30. This way, dihydro-β-agarofurans would obstruct the entrance of the substrate to the active site. The PAS is responsible for non-cholinergic functions of AChE and plays a role in the deposition of amyloid plaque. Therefore, molecules that bind to PAS site could, plays an important role slowing down the progression of AD31.