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    Degradation of Amino Acids: Presented By: Anuradha Verma

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    Qamar Qamar
    The document discusses the degradation of amino acids. It begins by providing background on amino acid structure and classification. It then describes three main pathways for amino acid degradation: transamination, which converts amino acids to keto acids; urea cycle, which occurs in the liver to convert ammonia into urea for excretion; and breakdown directly to intermediates of the citric acid cycle or gluconeogenesis. Key enzymes and cofactors involved in each degradation pathway are outlined. The document concludes by giving examples of degradation pathways for several specific amino acids.

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    Degradation of Amino Acids: Presented By: Anuradha Verma

    Uploaded by

    Qamar Qamar
    51 views46 pages
    The document discusses the degradation of amino acids. It begins by providing background on amino acid structure and classification. It then describes three main pathways for amino acid degradation: transamination, which converts amino acids to keto acids; urea cycle, which occurs in the liver to convert ammonia into urea for excretion; and breakdown directly to intermediates of the citric acid cycle or gluconeogenesis. Key enzymes and cofactors involved in each degradation pathway are outlined. The document concludes by giving examples of degradation pathways for several specific amino acids.

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    Knowledge for all

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    Knowledge for all

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    The document discusses the degradation of amino acids. It begins by providing background on amino acid structure and classification. It then describes three main pathways for amino acid degradation: transamination, which converts amino acids to keto acids; urea cycle, which occurs in the liver to convert ammonia into urea for excretion; and breakdown directly to intermediates of the citric acid cycle or gluconeogenesis. Key enzymes and cofactors involved in each degradation pathway are outlined. The document concludes by giving examples of degradation pathways for several specific amino acids.

    Copyright:

    © All Rights Reserved
    Download as PPT, PDF, TXT or read online from Scribd
    Download as ppt, pdf, or txt
    51 views46 pages

    Degradation of Amino Acids: Presented By: Anuradha Verma

    Uploaded by

    Qamar Qamar
    The document discusses the degradation of amino acids. It begins by providing background on amino acid structure and classification. It then describes three main pathways for amino acid degradation: transamination, which converts amino acids to keto acids; urea cycle, which occurs in the liver to convert ammonia into urea for excretion; and breakdown directly to intermediates of the citric acid cycle or gluconeogenesis. Key enzymes and cofactors involved in each degradation pathway are outlined. The document concludes by giving examples of degradation pathways for several specific amino acids.

    Copyright:

    © All Rights Reserved
    Download as PPT, PDF, TXT or read online from Scribd
    Download as ppt, pdf, or txt
    of 46

    Degradation of Amino Acids

    Presented By:
    Anuradha Verma
    What are amino acids?
    Proteins are polymers of amino acids, with each amino acid
    residue joined to its neighbor by a specific type of covalent
    bond.
    (The term “residue” reflects the loss of the elements of
    water when one amino acid is joined to another.)
    General Structure of Amino Acid

    This structure is common to all (except Proline, a cyclic amino acid).


    The R group or side chain (blue) attached to the carbon (green) is
    different in each amino acid.
     Asparagine was the first

    discovered amino acid in 1806.

     The last discovered was

    threonine in 1938.
    Structural Classification
    of Amino Acids
    1. With aliphatic side chains (Gly, Ala, Val, Leu, Ile)
    2. With side chain containing –OH group (Ser, Thr)
    3. With side chain containing S atom (Cys, Met)
    4. With side chain containing acid groups (Asp, Asn, Glu, Gln)
    5. Basic amino acids (His, Lys, Arg)
    6. Side chain having aromatic ring (Phe, Tyr, Trp)
    7. Secondary amino acid (Pro)
    The amino acid residues in protein molecules are exclusively L
    stereoisomers.
     D-Amino acid residues have been found only in a few, generally small
    peptides, including some peptides of bacterial cell walls and certain
    peptide antibiotics.
    Degradation of Amino Acids
     Ammonotelic:
    Releases ammonia as excretory product.
    e.g., aquatic vertebrates, bony fishes and larvae
    of amphibia.
     Ureotelic:
    Releases urea as excretory product.
    e.g., Terrestial vertebrates
     Uricotelic:
    Releases uric acid as excretory product.
    e.g., birds, reptiles
    Transamination reaction

    Most common amino acids can be converted into


    the corresponding keto acid by transamination.
    Pyridoxal Phosphate (PLP)
    and Aminotransferases
    PLP participate in the transfer of α-amino group to α-
    ketoglutarate leaving behind α-keto acid analog of amino acid in
    the presence of enzymes
    (transaminase / aminotransferases having prosthetic group -
    pyridoxal phosphate (PLP)

    Pyridoxal phosphate functions as an intermediate carrier


    of amino groups at the active site of aminotransferases.
    It undergoes reversible
    transformations between
    1- aldehyde form
    (pyridoxal phosphate)
    -which can accept an amino
    group and
    2- aminated form
    (pyridoxamine phosphate)
    -which can donate its amino
    group to an -keto acid
    Reactions at the - carbon include-
     Racemizations (interconverting L- and D-amino acids)
     Decarboxylations
     Transaminations
    Role of Pyridoxal phosphate:
    As bond to the - carbon of the substrate is broken, removing
    either a proton or a carboxyl group. The electron pair left
    behind on the α-carbon would form a highly unstable
    carbanion. Then, pyridoxal phosphate provides resonance
    stabilization of this intermediate. The highly conjugated
    structure of PLP (an electron sink) permits delocalization of the
    negative charge.
    Glutamate Releases Its Amino
    Group as Ammonia in the Liver
    Classification of amino acid on
    the basis of their end products
     Glucogenic
    Glucogenic amino acids are those that give rise to a net
    production of pyruvate or TCA cycle intermediates,
    such as α-ketoglutarate or oxaloacetate, all of which
    are precursors to glucose via gluconeogenesis.
     Ketogenic
    Ketogenic are those which degrades to give
    acetoacetate or acetyl CoA.
    e.g., Leucine & lysine
     Both glucogenic & ketogenic
    e.g., Phenylalanine, Tyrosine, Tryptophan, Isoleucine
    Urea cycle
     In ureotelic organisms, the ammonia deposited
    in the mitochondria of hepatocytes is
    converted to urea in the urea cycle.

     This pathway was discovered in 1932 by Hans


    Krebs and Kurt Henseleit.

     Urea production occurs almost exclusively in


    the liver.
    I step
     The first amino group to enter the urea cycle is derived from
    ammonia in the mitochondrial matrix—NH4+
     The NH4 generated in liver mitochondria is immediately
    used, together with CO2 (as HCO3) produced by
    mitochondrial respiration, to form carbamoyl phosphate in
    the matrix .
     This ATP-dependent reaction is catalyzed by carbamoyl
    phosphate synthetase I.
    II Step
     The carbamoyl phosphate functions as an activated
    carbamoyl group donor enters the urea cycle.
     Carbamoyl phosphate donates its carbamoyl group to
    ornithine to form citrulline, with the release of Pi. The
    reaction is catalyzed by ornithine transcarbamoylase.

     Citrulline passes from the mitochondrion to the cytosol


    III Step
    Second amino group now enters from aspartate (generated
    in mitochondria by transamination and transported into
    the cytosol) by a condensation reaction between the
    amino group of aspartate and the ureido (carbonyl) group
    of citrulline, forming argininosuccinate, catalyzed by
    argininosuccinate synthetase, requires ATP.
    IV Step
     Argininosuccinate is then cleaved by
    argininosuccinase to form free arginine and
    fumarate
     fumarate enters mitochondria to join the pool of
    citric acid cycle intermediates.
    V Step
    Arginasecleaves arginine to yield urea and
    ornithine.
    Ornithine is transported into the mitochondrion
    to initiate another round of the urea cycle.
    Glutamic Acid:
    • glutamate dehydrogenase
    Glutamine:
    glutaminase
    Glu

    Proline:

    Glutamate Gamma-semi aldehyd


    Arginine:

    H2N

    Ornithine aminotransferase

    Glu-5-semiald.
    DH
    Histidine:
    histidine
    ammonia
    lyase

    U r o c o n a t e h y d r a ta s e

    H
    im i d a z o l o n e p r o p i o n a s e

    HN

    N-fo
    Glutamate foriminotransferase

    Glutam

    Here glutamate foriminotransferase transfer


    the forimino group to THF
    How Propionyl CoA converting to Succinyl CoA

    I.step enzyme- Propionyl CoA carboxylase


    II.step enzyme- Mutase
    Valine:

    Valine transaminase PLP


    alpha KGA Glu

    H2 O
    Dehydogenase
    alpha-keta NAD
    isovaleric
    acid DH NADH+
    H+

    isobutaryl CoADH

    enoyl CoAhydratase
    Trypt
    Asparagine and Aspartic Acid:

    Asparaginase

    Catalysed by aspartate amino transferase.


    Alanine:
    Catalysed by alanine amino transferase
    Serine:
    Serine
    dehyratas
    e
    cofactor
    β-el
    am
    imine
    S e r. d e h y d ra ta s e

    pyruva
    T a u to m e riza tio n

    NH3
    H2O

    P yru v ic A c id
    References
    • Principles of Biochemistry, Lehninger
    • Concise Textbook of Chemistry, G.Rajagopal
    • www.tamu.edu/faculty/bmiles/lectures/amcat
    .pdf - United States
    • www.rpi.edu/dept/bcbp/molbiochem/MBWeb/
    mb2/.../aacarbon.htm
    • www.bmb.leeds.ac.uk/illingworth/metabol/ami
    no.htm

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