PPT-Diseases of Amino Acid Metabolism-I

VBC607 UnitI PG 31102020 DEFECT IN AMINO ACID CATABOLISM Phenylketonuria Deficiency of phenylalanine hydroxylase or a defect in biosynthesis reduction of tetrahidrobiopterin. . Cytochrome C in Humans Compared to Other Species Using Bioinformatics. We live in a human-centric world.. Human Metabolism. Sugar +. O. xygen. Energy!. Aerobic respiration. 1. Glycolysis. 2. Citric acid cycle. 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. 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). 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 . 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. . 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: . 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: . 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.. 1. Important. .. Extra Information.. Doctors slides. 436 Biochemistry team. One day or day one you decide ... By the end of this lecture the students will be able to:. • Identify the amino acid degradation and synthesis of non-essential amino acids..