It's very good question It's because,most of the transaminases are specific to alpha Ketoglutarate . Explanation: so,when transamination takes place ,alpha KGA is converted into Glutamate.This is the form in which amino group is carried to liver, where it is used for synthesis of urea or non-essential amino acids. Ammonia is Neurotoxic ,that's why it's levels should be maintained in low concentrations in blood and that is possible only with the transport of ammonia in the form of Glutamate.And for the formation of Glutamate, Alpha Keto Glutarate is required. And most transaminases they have specificity to Alpha KGA.
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Why there is a specific enzyme only for glutamate deamination
It's very good question
It's because,most of the transaminases are specific to alpha Ketoglutarate .
Explanation:
so,when transamination takes place ,alpha KGA is converted into Glutamate.This is the form in which amino group is carried to liver, where it is used for synthesis of urea or non-essential amino acids.
Ammonia is Neurotoxic ,that's why it's levels should be maintained in low concentrations in blood and that is possible only with the transport of ammonia in the form of Glutamate.And for the formation of Glutamate, Alpha Keto Glutarate is required.
And most transaminases they have specificity to Alpha KGA.
@@biochemistryconcepts ty so much for the Explanation
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Thankyou sir clearly explained 🙏👍
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