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, a process that has been confirmed in multiple studies. Interestingly, tdc exhibits specificity in that it cannot utilize other aromatic L-amino acids, such as L-phenylalanine, L-tryptophan, and L-glutamic acid, 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. The total length of tdc Protein, Levilactobacillus brevis (FLAG, His) is 626 a.a., .

The tdc protein is an enzyme that catalyzes the decarboxylation of L-tyrosine to produce tyramine. This enzymatic activity is crucial for the conversion of tyrosine into tyramine, a process that contributes to the biosynthesis of various biologically active amines. Importantly, tdc exhibits specificity towards L-tyrosine and cannot utilize other aromatic L-amino acids such as L-phenylalanine, L-tryptophan, and L-glutamate as substrates. Notably, tdc can also decarboxylate levodopa (L-dopa), a medication used in the treatment of Parkinson's disease, to produce dopamine in vitro. This broader substrate specificity suggests potential implications for tdc in neurotransmitter synthesis and pharmaceutical applications, particularly in the context of Parkinson's disease therapy.

Others

E. coli

N-6*His;N-Flag

J7GQ11 (M1-V626)

/

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

<1 EU/μg, determined by LAL method.