Protein metabolism

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Protein metabolism

  1. 1. PROTEINS AMINO ACIDS, STRUCTURE, FUNCTIONS & METABOLIC PATHWAYS
  2. 2. WHAT IS PROTEIN METABOLISM?!!?
  3. 3. ` Protein metabolism denotes the various biochemical processes responsible for the synthesis of proteins and amino acids?, and the breakdown of proteins (and other large molecules, too) by catabolism.
  4. 4.  Proteins contain carbon, hydrogen, oxygen, nitrogen , and sometimes other atoms. They form the cellular structural elements, are biochemical catalysts, and are important regulators of gene expression .  Nitrogen is essential to the formation of twenty different amino acids, the building blocks of all body cells. Amino acids are characterized by the presence of a terminal carboxyl group and an amino group in the alpha position, and they are connected by peptide bonds.
  5. 5.  Digestion breaks protein down to amino acids. If amino acids are in excess of the body's biological requirements, they are metabolized to glycogen or fat and subsequently used for energy metabolism.  If amino acids are to be used for energy their carbon skeletons are converted to acetyl CoA, which enters the Krebs cycle for oxidation, producing ATP. The final products of protein catabolism include carbon dioxide, water, ATP, urea, and
  6. 6. AMINO ACID SYNTHESIS  Amino acid synthesis is the set of biochemical processes ( metabolic pathways) by which the various amino acids are produced from other compounds.  Amino acids are critical to life, and have a variety of roles in metabolism. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesise all amino acids, for example
  7. 7. AMINO ACIDS  Amino acids are molecules containing both amine and carboxyl functional groups. These molecules are particularly important in biochemistry, where this term refers to alphaamino acids with the general formula H2NCHRCOOH, where R is an organic substituent.  In the alpha amino acids, the amino and carboxylate groups are attached to the same carbon atom, which is called the α–carbon. The various alpha amino acids differ in which side chain (R group) is attached to their alpha carbon. They can vary in size from just a hydrogen atom in glycine through a methyl
  8. 8.  At pH of 7, amino group is protonated (-NH3+) and carboxyl group is ionized (COO-). The amino acid is called a zwitterion.  The a carbon is chiral or asymmetric ( 4 different groups are attached to the carbon; exception is glycine.)  Amino acids exist as stereoisomers (same molecular formula, but differ in arrangement of groups). Designated D(right) or L(left). Amino acids used in nature are of L configuration. carboxylate group at top --> points away side chain at

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