Pyridoxal-phosphate (PLP, pyridoxal-5'-phosphate, P5P) is a prosthetic group of some enzymes. It is the active form of vitamin B6 which comprises three natural organic compounds, pyridoxal, pyridoxamine and pyridoxine.
Additionally, 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.
It is also active in the condensation reaction in heme synthesis.
Pyridoxal phosphate is not required in the transaminase reaction of lysine catabolism.
PLP allows the conversion of the excitatory neurotransmitter Glutamate to the inhibitory neurotransmitter GABA.
PLP allows the conversion of histidine to histamine via decarboxylation.
Although the vast majority of PLP-dependent enzymes form an internal aldimine with PLP via an active site lysine residue, some PLP-dependent enzymes do not have this lysine residue, but instead have an active site histidine. In such a case, the histidine cannot form the internal aldimine and therefore the cofactor never becomes covalently tethered to the enzyme. GDP-4-keto-6-deoxymannose-3-dehydratase (ColD) is an example of such an enzyme .
Pyridoxal phosphate and hepatocyte growth factor prevent dialysate-induced peritoneal damage.(Pyridoxal-5'-Phosphate)(Report)
Jul 01, 2009; Glucose-based peritoneal dialysate (PD) is responsible for increased accumulation of advanced glycation end products (AGE) in the...