Pyridoxal Phosphate - Role As A Coenzyme

Role As A Coenzyme

PLP acts as a coenzyme in all transamination reactions, and in some decarboxylation and deamination reactions of amino acids. The aldehyde group of PLP forms a Schiff-base linkage (internal aldimine) with the ε-amino group of a specific lysine group of the aminotransferase enzyme. The α-amino group of the amino acid substrate displaces the ε-amino group of the active-site lysine residue. The resulting external aldimine becomes deprotonated to become a quinoid intermediate, which in turn accepts a proton at a different position to become a ketimine. The resulting ketimine is hydrolysed so that the amino group remains on the complex.

In addition, PLP is used by aminotransferases (or transaminases) that act upon unusual sugars such as perosamine and desosamine. In these reactions, the PLP reacts with glutamate, which transfers its alpha-amino group to PLP to make pyridoxamine phosphate (PMP). PMP then transfers its nitrogen to the sugar, making an amino sugar.

PLP is also involved in various beta-elimination reactions such as the reactions carried out by serine dehydratase and GDP-4-keto-6-deoxymannose-3-dehydratase (ColD).

It is also active in the condensation reaction in heme synthesis.

PLP plays a role in the conversion of dopa into dopamine, allows the conversion of the excitatory neurotransmitter glutamate to the inhibitory neurotransmitter GABA, and allows SAM to be decarboxylated to form propylamine, which is a precursor to polyamines.

Read more about this topic:  Pyridoxal Phosphate

Famous quotes containing the word role:

    Where we come from in America no longer signifies—it’s where we go, and what we do when we get there, that tells us who we are.
    The irony of the role of women in my business, and in so many other places, too, was that while we began by demanding that we be allowed to mimic the ways of men, we wound up knowing we would have to change those ways. Not only because those ways were not like ours, but because they simply did not work.
    Anna Quindlen (b. 1952)