PPT-Diseases of amino acid metabolism- II

VBC607 Unit1 PG 6112020 MAPLE SYRUP URINE DISEASE Also known as Branched chain ketonuria Partial or complete deficiency of branchedchain α keto acid dehydrogenase a multienzyme complex associated with inner membrane of mitochondrion. What are amino acids?. Amino acids are the building blocks of proteins.. In the body, they exist as zwitterions.. Zwitterions can behave as both an acid or a base.. Today we will:. Study . the acid-base properties of amino acids, . 15 . Slides. AMINO ACID . CATABOLISM. fig 18-1. fate of amino nitrogen in mammals. fig 18-2. metabolism of amino nitrogen in liver. fig 18-2. nitrogen removal molecules…. fig 18-2. metabolism of amino nitrogen in liver. Grant . Alex . Curtis. Why?. The purpose of this study was to examine the net hormonal effect of amino acid supplementation on the overreaching resistance training-induced hormonal stress response.. Variables. Formation of Aminoacyl tRNAs. Ribosome structure. Stages of Translation. Relationship between DNA, mRNA, and Protein Sequences. Translation and the Genetic Code. Amino acid structure. Four different groups are attached to the central carbon atom (. Chapter 30, . Stryer. Short Course. Overview. Amino Acid Catabolism. Nitrogen removal. Urea Cycle. Metabolism of carbon backbone. Amino acid catabolism. Amino acids . from diet or protein turnover. Salvaged for use in proteins or catabolized. Stryer. Short Course, Chapter 31. Nitrogen fixation. Bacteria. Nitrogenase. Costly—16 ATP per N. 2. molecule. Assimilation into Amino Acids. In microorganisms/plants: assimilation of ammonia is key—synthesis of most amino acids. Nitrogen Metabolism. Nitrogen Forms in the Body. Nitrogen Balance Critical. Body Must Make and Break Down Amino Acids. Nitrogen Also Needed for Synthesis of. Nucleotides (ATP, GTP, CTP, UTP, dATP, dCTP, dGTP, dTTP). . are organic molecules that are the building block of . . proteins. .. -There is 20 . α. -amino acids commonly found in . proteins. . ( . they . have a carboxyl group and an amino group . . . Peptide bond formation. : . α-carboxyl group of one amino acid (with side chain R1) forms a covalent peptide bond with α-amino group of another amino acid . ( . with the side chain R2) by removal of a molecule of water. The result is : Dipeptide ( i.e. Two amino acids linked by one peptide bond). By the same way, the dipeptide can then forms a second peptide bond with a third amino acid (with side chain R3) to give . GLYCINE. Glycine is the . simplest . amino acid. Chemically it is “. amino acetic acid. . ".. It is non-essential amino acid and can be synthesized in . tissues. . Though it is non- essential but it is an important amino acid as it forms many biologically important compounds in the body.. Unit-1. P.G.. 25.09.2020. Oxidative Deamination . L-AA oxidase and D-AA oxidase act on L-AA and D-AA respectively and oxidatively removes NH. 3. from AA.. Glutamate formed by transamination reactions is deaminated to . (N. utritionally. . Essential & Nutritionally Non Essential Amino . Acids ). Lecture : 4. Dr. . Shaimaa. . Munther. Nutritionally Essential & Nutritionally Non Essential Amino Acids . Introduction: . Class- . Bsc bioscience 6. th. semester. Section – . D. Introduction. Amino acid are the currency of of nitrogen and protein economy of the host, hence they are used in many pathways beyond protein synthesis, including energy production and neurotransmitter synthesis.. Daum LT, Canas LC, Smith CB, Klimov A, Huff W, Barnes W, et al. Genetic and Antigenic Analysis of the First A/New Caledonia/20/99-like H1N1 Influenza Isolates Reported in the Americas. Emerg Infect Dis. 2002;8(4):408-412. https://doi.org/10.3201/eid0804.010311.