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  Oxidative deamination

Oxidative deamination:

The meaning of deamination is elimination of the amino groups from amino acids. This is the technique where in the amino acids lose two hydrogen atoms (dehydrogenation) to create ammonia and keto acids.

Oxidative deamination is accompanied via oxidation and is catalysed through particular amino acid oxidases or more correctly, dehydrogenases available in liver and kidneys. The procedure of oxidative deamination occurs in two steps.

The 1st step is oxidation (dehydrogenation) of amino acid resultant in the creation of imino acid. After that the imino acid goes through the second step that is hydrolysis that results in a keto acid and ammonia.

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The first reaction is catalyzed via amino acid oxidase (as well called dehydrogenase) and the coenzyme FAD or FMN starts the hydrogen. There are two kinds of amino acid oxidases relies on the substrate, on which they work, that is:

1. L-amino acid oxidases that act on L-amino acids (FMN works as coenzyme).
2. D-amino acid oxidases that act on D-amino acids (FAD works as coenzyme).

FMN takes place only in the liver and kidney and FAD takes place in all animal tissues. The main site of oxidative deamination is liver however kidney and other tissues as well have a role.

The L-glutamic acid’s oxidative deamination is an exceptional case in which the deamination requires not only the zinc- that containing enzyme L-glutamic acid dehydrogenase but as well NAD+ or NADP+ as coenzymes.

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NADH oxidized to NAD+ as it passes via the electron transport chain.

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Like the above reaction is reversible it takes place during both amino acid catabolism and biosynthesis.

 

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