L-Tyrosine decarboxylase from Streptococcus faecalis has been used in a study to isolate and identify the carbonyl-active site of diamine oxidase by gas chromatographic mass spectrometry. L-Tyrosine decarboxylase from Streptococcus faecalis has also been used in a study to investigate the adsorption of Streptococcus faecalis on diatomite carriers for use in biotransformations.
Biochem/physiol Actions
L-Tyrosine Decarboxylase Apoenzyme is an aromatic L-amino acid decarboxylase. The enzyme activity of tyrosine decarboxylase (TDC) is dependent on the cofactor pyridoxal 5-phosphate (PLP). It catalyzes the decarboxylation of dihydroxyphenylalanine.
