Tyrosine decarboxylase transamination

Pyridoxamine phosphate serves as a coenzyme of transaminases, e.g., lysyl oxidase (collagen biosynthesis), serine hydroxymethyl transferase (Cl-metabolism), S-aminolevulinate synthase (porphyrin biosynthesis), glycogen phosphoiylase (mobilization of glycogen), aspartate aminotransferase (transamination), alanine aminotransferase (transamination), kynureninase (biosynthesis of niacin), glutamate decarboxylase (biosynthesis of GABA), tyrosine decarboxylase (biosynthesis of tyramine), serine dehydratase ((3-elimination), cystathionine 3-synthase (metabolism of methionine), and cystathionine y-lyase (y-elimination). 

One of the earliest published attempts to create antibodies with catalytic activity had as its goal the generation of a transaminase. Raso and Stollar prepared V-(5-phosphopyridoxyl)-3 -amino-L-tyrosine 154 as a mimic of the Schiff s base intermediate that is formed during the pyridoxal-dependent transamination of tyrosine and showed that it was a site-directed inhibitor of the enzymes tyrosine transaminase and tyrosine decarboxylase.132 Partially purified polyclonal antibodies, elicited against y-globulin conjugates of the hapten, recognized both the... 

The conversion of pyridoxal to pyridoxamine in heat-sterilized media was confirmed to be due to the reaction of pyridoxal with amino acids (Snell 1945). This was the first discovery of nonenzymatic transamination. The transamination reaction in animal tissues was first discovered in 1937 by Alexander Braunstein and associates as an amino group transfer between glutamate and alanine in pigeon muscle extract (Braunstein 1939). Irwin Gunsalus and associates showed that the tyrosine decarboxylase activity of S. faecalis was... 

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