PPT-Amino Acid Degradation and Synthesis

UNIT IV Nitrogen Metabolism Part 3 Neonatal screening and diagnosis of PKU Early diagnosis of phenylketonuria is important because the disease is treatable by dietary means Because of the lack of neonatal symptoms laboratory testing for elevated blood levels of phenylalanine is mandatory for detection . C483 Spring 2013. Questions. 1. The . primary structure of a protein specifically describes the ________. . A. ) location of disulfide bonds. B. ) linear sequence of amino acids . C. ) overall three-dimensional shape . 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. 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). Plants and bacteria produce all of their amino acids using NH. 4. +. and NO. 3. –. .. Humans can synthesize 9 of the 20 amino acids found in their proteins.. Nonessential amino acids are synthesized in the body, while essential amino acids must be obtained from diet.. 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 (. 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 . (. N-. Catabolisim. of Amino Acid). *. transamination. *Deamination(oxidative or nonoxidative. . deamination. ). *Transdeamination. * NH. 3. transport . *formation of urea. .. . Transamination. *Transamination means transfer of amino group from α-amino acid to α-. 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.. 2. Aged proteins, damaged or modified proteins and non-functional proteins of the body undergo degradation. . 3. Protein degradation may play important role in shaping tissues and organs during pregnancy and development.. (N. utritionally. . Essential & Nutritionally Non Essential Amino . Acids ). Lecture : 4. Dr. . Shaimaa. . Munther. Nutritionally Essential & Nutritionally Non Essential Amino Acids . Introduction: . The function of the different types of RNA in the cell is to facilitate the task of synthesizing proteins.. An activated . tRNA. with anticodon AGU bonds to serine at the acceptor stem.. Learning Goal .