PPT-Catabolism of amino acids

The general ways of amino acids degradation Transamination Deamination Decarboxylation The major site of amino acid degradation the liver BIOSYNTHESIS OF UREA Urea biosynthesis occurs in four stages . 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 . (Foundation Block). Dr. Ahmed Mujamammi. Dr. . Sumbul. . Fatma. Learning outcomes. What are the amino acids?. General structure.. Classification of amino acids.. Optical properties.. Amino acid configuration.. 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.. B.2. Properties of 2-amino acids . (B.2.2). Zwitterion. (dipolar) . amino acids contain both acidic and basic groups in the same molecule . therefore, are . amphoteric. in nature (capable of behaving as acids or bases). 18. /2014. Biochemistry I. Dr. Loren Williams. Proteinogenic Amino Acids. An amino acid contains . an amine group . a carboxylic acid group, . a side-chain (or R-group,. all attached to the same chiral carbon atom (the Cα). DR AMINA . BIOCHEMISTRY. All tissues have some capability for synthesis of:. The non-essential amino acids,. Amino acid remodeling, . and Conversion of non-amino acid carbon skeletons into amino acids and other derivatives that contain nitrogen. . amine group. Draw. a carboxylic acid group. Join. them together to form a molecule with an amine and . a carboxylic acid . group. Amino Acids. Building blocks of proteins. Two functional groups: a carboxylic acid and a primary amine. 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 . 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.. u. sing paper chromatography. Kate Andrews. Lorraine Bruce. Unit 1 DNA and the Genome. 3 Control of gene expression. Separation and identification of amino acids using paper chromatography.. Cells and Proteins. Prepared by. Harpreet Malhotra. Florida State College at Jacksonville. 24.1 Introduction (1). In the catabolism of . carbohydrates. , . glycolysis. converts . glucose. . into . pyruvate. , which is then metabolized into .