tdc Protein, Levilactobacillus brevis (FLAG, His)

TDC protein plays a key role in amino acid metabolism by catalyzing the decarboxylation of L-tyrosine to produce tyramine. TDC is specific and does not utilize other aromatic L-amino acids such as L-phenylalanine, L-tryptophan, and L-glutamate as substrates. tdc Protein, Levilactobacillus brevis (FLAG, His) is the recombinant tdc protein, expressed by E. coli , with N-6*His, N-Flag labeled tag.

TDC protein is an enzyme that catalyzes the decarboxylation of L-tyrosine to produce tyramine. This enzymatic activity is essential for the conversion of tyrosine to tyramine, a process that contributes to the biosynthesis of various bioactive amines. Importantly, TDC exhibits specificity for L-tyrosine and is unable to utilize other aromatic L-amino acids such as L-phenylalanine, L-tryptophan, and L-glutamate as substrates. TDC can also decarboxylate L-dopa (L-dopa), a drug used to treat Parkinson's disease, to produce dopamine in vitro. This indicates the potential impact of TDC in neurotransmitter synthesis and pharmaceutical applications, especially in the treatment of Parkinson's disease.

Others

E. coli

N-6*His;N-Flag

J7GQ11 (M1-V626)

/

Full Length

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.