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    Deamination of Amino Acids - The Urea Cycle

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    Lei ぱんがにばん
    This document discusses the urea cycle and oxidative deamination reactions. The urea cycle converts ammonia produced from amino acid breakdown into urea in the liver, which is then excreted by the kidneys. Glutamate is a key intermediate that receives amino groups from other amino acids via transamination reactions, allowing their deamination and incorporation of nitrogen into urea. Enzymes in the urea cycle are regulated to eliminate excess nitrogen from high-protein diets.

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    Deamination of Amino Acids - The Urea Cycle

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    Lei ぱんがにばん
    172 views4 pages
    This document discusses the urea cycle and oxidative deamination reactions. The urea cycle converts ammonia produced from amino acid breakdown into urea in the liver, which is then excreted by the kidneys. Glutamate is a key intermediate that receives amino groups from other amino acids via transamination reactions, allowing their deamination and incorporation of nitrogen into urea. Enzymes in the urea cycle are regulated to eliminate excess nitrogen from high-protein diets.

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    Deamination(s)

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    This document discusses the urea cycle and oxidative deamination reactions. The urea cycle converts ammonia produced from amino acid breakdown into urea in the liver, which is then excreted by the kidneys. Glutamate is a key intermediate that receives amino groups from other amino acids via transamination reactions, allowing their deamination and incorporation of nitrogen into urea. Enzymes in the urea cycle are regulated to eliminate excess nitrogen from high-protein diets.

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    Download as DOCX, PDF, TXT or read online from Scribd
    Download as docx, pdf, or txt
    172 views4 pages

    Deamination of Amino Acids - The Urea Cycle

    Uploaded by

    Lei ぱんがにばん
    This document discusses the urea cycle and oxidative deamination reactions. The urea cycle converts ammonia produced from amino acid breakdown into urea in the liver, which is then excreted by the kidneys. Glutamate is a key intermediate that receives amino groups from other amino acids via transamination reactions, allowing their deamination and incorporation of nitrogen into urea. Enzymes in the urea cycle are regulated to eliminate excess nitrogen from high-protein diets.

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    

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     
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    

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    DEAMINATION OF AMINO ACIDS – The Urea Cycle

    Urea is the major end product of nitrogen metabolism in humans and mammals. Ammonia,
    the product of oxidative deamination reactions, is toxic in even small amounts and must be removed
    from the body. The urea cycle or the ornithine cycle describes the conversion reactions of ammonia
    into urea. Since these reactions occur in the liver, the urea is then transported to the kidneys where it
    is excreted. The overall urea formation reaction is:

    2 Ammonia + Carbon dioxide (CO2) + 3 ATP urea + water (H2O) + 3 ADP

    The essential features of the urea cycle reactions and their metabolic regulation are as follows:
    Arginine from the diet or from protein breakdown is claved by cystosolic enzyme arginase,
    generating the urea and ornithine. In subsequent reactions of the urea cycle a new urea residue is
    built on the ornithine, regenarating arginine and perpetuating the cycle.

    Regulation of the Urea Cycle


    The urea cycle operates only to eliminate excess nitrogen. On high-protein diets the carbon
    skeletons of the amino acids are oxidized for energy or stored as fat and glycogen, but the amino
    nitrogen must be excreted. To facilitate this process, enzymes of the urea cycle are controlled at the
    gene level.
    

    Deamination is also an oxidative reaction that occurs


    under aerobic conditions in all tissues but especially the
    liver. During oxidative deamination, an amino acid is
    converted into the corresponding keto acid by the
    removal of the amine functional group as ammonia and
    the amine functional group is replaced by the ketone
    group. The ammonia eventually goes into the urea cycle.

    Oxidative deamination occurs primarily on glutamic acid


    because glutamic acid was the end product of many
    transamination reactions.

    The glutamate dehydrogenase is allosterically controlled


    by ATP and ADP. ATP acts as an inhibitor whereas
    ADP is an activator.

    CENTRAL ROLE FOR GLUTAMIC ACID:

    Apparently most amino acids may be deaminated but


    this is a significant reaction only for glutamic acid. If
    this is true, then how are the other amino acids
    deaminated? The answer is that a combination of
    transamination and deamination of glutamic acid
    occurs which is a recycling type of reaction for
    glutamic acid. The original amino acid loses its amine
    group in the process. The general reaction sequence is
    shown on the left.
    TRANSAMINATION REACTION

    O O O O

    CH3 – CH – C – OH + HO-C-CH2-CH2-C-C-OH

    Alanine alpha-ketoglutaric acid

    ______________________________________________________________

    O O O O

    CH3 – C – C – OH + HO-C-CH2-CH2-CH-C-OH

    Pyruvic acid glutamic acid

    Transamination refers to the transfer of an amine group from one molecule to another. This reaction
    is catalyzed by a family of enzymes called transaminases. Transamination reaction results in the exchange of
    an amine group on one acid with a ketone group on another acid. It is analogous to a double replacement
    reaction.

    The most usual and major keto acid involved with transamination reactions is alpha-ketoglutaric acid, an
    intermediate in the citric acid cycle.

    A specific example is the transamination of alanine to make pyruvic acid and glutamic acid. Other
    amino acids which can be converted after several steps through transamination into pryruvic acid include,
    serine, cysteine and glycine.

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