TRANSAMINATION
- It is a chemical reaction where an amino group from an amino
acid is removed and transfers to a ketoacid, resulting in the
formation of a new aminoacid.
- deamination of most aminoacids happens this way
- it converts essential aminoacids to non-essential
aminoacids
- catalysed by the enzyme transaminases or aminotransferases
- aminotransferases are specific for individual aminoacids. most
common ones are Alanine aminotransferase and aspartate
aminotransferase
- lysine, proline and threonine do not always undergo
transamination
the reaction is as follows,
Aminoacid +
alpha-ketoglutarate <-------> alpha-keto acid +
glutamate
OXIDATIVE DEAMINATION
- occurs only in liver
- generates alpha keto acids and other oxidised products
- generate ammonia as a toxic byproduct, that enters urea cycle
and get neutralised
- enzyme involved is dehydrogenase ( which use NAD or NADP as
coenzyme) and oxidase
- it differs from transamination in that it loses the amino group
instead of trasfering it to another amino acid
the reaction,
Glutamate + NAD+ + H2O
<--------(glutamate dehydrogenase)---------> alpha-keto
glutarate + NH+4 + NADH
Role of pyridoxal phosphate (PLP) :-
- it is an active form of vitamin B6 .
- it acts as a coenzyme in all transamination reactions and
certain deamination reactions.
- aldehyde group of PLP forms a schiff base linkage with amino
groups of amino acids
Glutamate :-
- as discussed already it is involved in transamination
- alpha keto glutarate accepts the amino group and form
glutamate
- this glutamate's amino group is again transfered to
oxaloacetate , yields aspartate
Glutamate + oxaloacetate
<---------------(glutamate degydrogenase)-------------->
alpha-keto glutarate + aspartate
Glutamate degydrogenase :-
- it is the enzyme invoved in the above reaction
- converts glutamate to alpha keto glutarate
Alpha keto glutarate :-
- it is one of the ketone derivatives of glutaric acid
- also called 2 oxo- glutarate
- it is an anion