PPT-1 Metabolism of Amino Acids. Part II

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. 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, . C483 Spring 2013. Questions. 1. . Amino acids with non-. ionizable. side chains are zwitterions when they are ________.. A. ) in any solution . . D) in alkaline solutions only . B. ) at physiological pH, pH = 7.4 . Codons. Prefixes, Suffixes and Vocabulary. Poly. = many. Peptide bond . =bond between two amino acids.. Anti. = against, opposite. Dehydration. = loss of water. Polypeptide. = long assembled string of amino acids.. CHAPTER 3, Part 1 . Amino Acids and Peptides . To know the structure and naming of all 20 protein amino acids. To know the structure and properties of peptides and the particularly the structure of the peptide bond.. Stryer. Short Course. Chapter . 3. Amino Acid Structure. Alpha carbon. Sidechain. Proteins. peptides. Stereochemisty. L-amino acids. Glycine. R/S . vs. D/L. L-isoleucine. racemization. Ionization of Amino Acids. THE EXCRETION OF AMMONIUM IONS. A part of NH4+ that is formed in the degradation of amino acids is used for the biosynthesis of nitrogen compounds. In most of the land living vertebrates the excess NH4+ is converted in urea and in that form is excreted. In birds and reptiles it is converted into uric acid and in aquatic animals it is directly excreted as urea.. When an amino acid with positive and negative charges is overall neutral in charge, it is said to be at its . isoelectric point (. pI. ). .. . Ball-and-stick model of glycine at its . pI. of 6.0.. 1. . Overview. The catabolism of the amino acids involves:. Removal of α-amino groups. . Breakdown of the resulting carbon skeletons.. The resulting compounds will be used to form seven intermediate products: . Amino acids are weak . polyprotic. acids . . Neutral amino acids are (. gly. , ala, threonine ) are treated as diprotic acids .. acidic amino acids (. glu. , asp,) are treated as . triprotic. acids .. 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 . Intermediary Metabolism. OR. Interrelationship Between Various Metabolic . Pathways. OR. Interdependence Of Metabolic Pathways. To Better Understand Metabolism Of Various Biomolecules . Metabolism of each . VBC-607. Unit-1. P.G.. 6.11.2020. MAPLE SYRUP URINE DISEASE. Also known as Branched chain ketonuria. Partial or complete deficiency of branched-chain . α . keto acid dehydrogenase (a multienzyme complex associated with inner membrane of mitochondrion). 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 BSc 3. rd. year . AMINO ACIDS. C. lassification of amino acids . Classification according to nature of side chain. PREPARATION OF AMINO ACIDS. 1. Gabriel Phthalimide synthesis. 2. Strecker’s synthesis.