PPT-1 Amino acidopathies: defects in amino acid metabolism

Richard D Howells PhD Dental Biochemistry Lecture 25 2 Learning Objectives To distinguish between phenylketonuria PKU caused by phenylalanine hydroxylase PAH defect and PKU caused by defect in . In the United States about 7200 or 18 per 10000 babies born every year have critical congenital heart defects CCHDs which also are known collectively in some instances as critical congenital heart disease These CCHDs are coarctation of the aorta do 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. 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 (. We live in a human-centric world.. Life exists outside our box.. Subtitle. Text. Shock & Holland (2007). For example, there is life deep down on the ocean floor.. C-DEBI . (Center for Deep Energy Biosphere Investigations). 1. Arginine is biosynthesized from this precursor:. Pyruvate. Oxaloacetate. . a. -. ketoglutarate. 3-phosphoglycerate. 2. A . Roundup Ready plant is one that has been genetically modified so that an enzyme (EPSP synthase) can no longer bind to the active ingredient (. What to Know. What is the Metabolic Fate of Ammonium?. How is Escherichia coli Glutamine Synthetase regulated?. Understand general ways that organisms synthesize amino acids. Know the definition of essential versus nonessential amino acids. Richard D. Howells, PhD. Dental Biochemistry Lecture 24. 2. Learning Objectives. To describe the urea cycle and its fundamental role in the excretion of nitrogen.. To . distinguish between . glucogenic. Learning Objectives :. 1. Know the groups of . a.a. . biosynthetic families. 2. The enzymes and coenzymes involved in the synthetic pathways. 3. The enzyme deficiencies of each pathway.. 4. The consequences of the inborn errors of metabolism. 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.. backbone.  . atoms . (see aminoAcids1).  but a unique set of . side chain . atoms. It's the side chains that make the 20 amino acids different from each other. . 1. Use the three identical backbone pieces and three unique side chain pieces below to construct three amino acids in the space to the right.. 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 . BC 2.5 Microbiology and Genetics 12 2 6 85 BC 2.6 Quantitative Analysis and Molecular Biology 12 2 6 85 BC 2.7 Viva-Voce -- 1 25 ----- Total marks unbranched. polymer chains composed of numerous small subunits or monomers is called amino acids .. There are 20 amino acids from which 18 have same structure.. DEFINATION. STRUCTURE. Amino acids have a central chiral carbon atom called alpha carbon. Groups attached to carbon atom are: .