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    Intro To Proteins Metabolism

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    Abdul Rauf
    Protein metabolism can be understood as the metabolism of amino acids. There is a pool of around 100g of free amino acids in the body that are maintained through input from digestion and output through various metabolic pathways. Amino acids undergo transamination and deamination. Transamination involves the transfer of amino groups between amino acids and keto acids, while deamination results in the liberation of ammonia. The carbon skeletons of amino acids are used for energy production, glucose synthesis, and the formation of fats or ketone bodies.

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    Intro To Proteins Metabolism

    Uploaded by

    Abdul Rauf
    17 views10 pages
    Protein metabolism can be understood as the metabolism of amino acids. There is a pool of around 100g of free amino acids in the body that are maintained through input from digestion and output through various metabolic pathways. Amino acids undergo transamination and deamination. Transamination involves the transfer of amino groups between amino acids and keto acids, while deamination results in the liberation of ammonia. The carbon skeletons of amino acids are used for energy production, glucose synthesis, and the formation of fats or ketone bodies.

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    Protein metabolism can be understood as the metabolism of amino acids. There is a pool of around 100g of free amino acids in the body that are maintained through input from digestion and output through various metabolic pathways. Amino acids undergo transamination and deamination. Transamination involves the transfer of amino groups between amino acids and keto acids, while deamination results in the liberation of ammonia. The carbon skeletons of amino acids are used for energy production, glucose synthesis, and the formation of fats or ketone bodies.

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    © All Rights Reserved
    Download as PPTX, PDF, TXT or read online from Scribd
    Download as pptx, pdf, or txt
    17 views10 pages

    Intro To Proteins Metabolism

    Uploaded by

    Abdul Rauf
    Protein metabolism can be understood as the metabolism of amino acids. There is a pool of around 100g of free amino acids in the body that are maintained through input from digestion and output through various metabolic pathways. Amino acids undergo transamination and deamination. Transamination involves the transfer of amino groups between amino acids and keto acids, while deamination results in the liberation of ammonia. The carbon skeletons of amino acids are used for energy production, glucose synthesis, and the formation of fats or ketone bodies.

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    © All Rights Reserved
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    Download as pptx, pdf, or txt
    of 10

    PROTEIN METABOLISM

    AN INTRODUCTION

    MRS. MUNAZA MAQSOOD


    LECTURER (BIOCHEMISTRY)
    INTRODUCTION

    • Proteins are the most abundant organic compounds and constitute a major
    part of the body dry weight (10-12 kg in adults).
    • Static (structural) and dynamic (enzymes, hormones, clotting factors, receptors
    etc.) functions.
    • About half of the body protein (predominantly collagen) is present in the
    supportive tissue (skeleton and connective) while the other half is intracellular

    • Degradation (proteolysis) release individual amino acids.


    • Amino acids undergoes its own metabolism and performs specific functions.
    INTRODUCTION
    • Some of the amino acids also serve as precursors for the
    synthesis of many biologically important compounds
    – e.g. melanin, serotonin, creatine etc.
    • Certain amino acids may directly act as neurotransmitters
    – e.g. glycine, aspartate, glutamate.

    Protein metabolism is more appropriately learnt as


    metabolism of amino acids.
    AMINO ACID POOL

    • An adult has about 100 g of free amino


    acids which represent the amino acid
    pool of the body.
    • Maintained by the sources that contribute
    (input) and the metabolic pathways that
    utilize (output) the amino acids
    • No storage form of amino acids
    • Digested by proteolytic enzymes to
    amino acids which are absorbed in the
    intestine and enter the body pool of
    amino acids
    METABOLISM OF AMINO ACIDS
    —GENERAL ASPECTS
    • The amino acids undergo transamination followed by
    deamination for the liberation of ammonia.
    • The amino group of the amino acids is utilized for the formation
    of urea which is an excretory end product of protein
    metabolism.
    • The carbon skeleton of the amino acids is first converted to keto
    acids (by transamination) which meet one or more of the
    following fates.

    1. Generate energy.
    2. Synthesis of glucose.
    3. Formation of fat or ketone bodies.
    4. Non-essential amino acids production

    A general picture of amino acid metabolism is


    depicted in Fig.
    TRANSAMINATION
    • The transfer of an amino ( NH2) group from an amino acid to a keto acid is
    known as transamination. This process involves the interconversion of a pair of
    amino acids and a pair of keto acids, catalysed by a group of enzymes called
    transaminases (recently, aminotransferases).
    Salient features of transamination

    1. All transaminases require pyridoxal phosphate (PLP),


    a coenzyme derived from vitamin B6.
    2. Specific transaminases exist for each pair of amino and
    keto acids. However, only two— namely, aspartate
    transaminase and alanine transaminase—make a
    significant contribution for transamination.
    3. There is no free NH3 liberated, only the transfer of
    amino group occurs.
    4. Transamination is reversible (Fig.
    DEAMINATION
    • The removal of amino group from the amino acids as NH3 is
    deamination. Transamination (discussed above) involves only the
    shuffling of amino groups among the amino acids. On the other hand,
    deamination results in the liberation of ammonia for urea synthesis.
    Simultaneously, the carbon skeleton of amino acids is converted to keto
    acids. Deamination may be either oxidative or non-oxidative.
    OXIDATIVE DEAMINATION

    Oxidative deamination is the liberation of free ammonia from the amino group of amino acids coupled
    with oxidation.
    This takes place mostly in liver and kidney. The purpose of oxidative deamination is to provide NH3 for
    urea synthesis and D-keto acids for a variety of reactions, including energy generation
    NON-OXIDATIVE DEAMINATION
    Some of the amino acids can be deaminated to liberate NH3 without undergoing oxidation

    • Amino acid dehydrases : Serine, threonine and homoserine are the hydroxy amino acids. They
    undergo non-oxidative deamination catalysed by PLP-dependent dehydrases (dehydratases).

    • Deamination of histidine : The enzyme histidase acts on histidine to liberate NH3 by a non-oxidative
    deamination process.

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