Tyrosine decarboxylase, Microorganism  (Synonyms: TDC; TyrDC)

Tyrosine decarboxylase, Microorganism (TDC) is a tyrosine decarboxylase produced by microorganisms. Tyrosine decarboxylase is a PLP-dependent enzyme that catalyzes the decarboxylation of L-tyrosine, L-phenylalanine, and L-dopa to produce tyramine, 2-phenethylamine, and dopamine, respectively. Tyrosine decarboxylase mediates acid stress resistance, maintains intracellular pH homeostasis, and generates proton motive force^[1][2].

Tyrosine decarboxylase is a PLP-dependent enzyme that catalyzes the decarboxylation of L-tyrosine, L-phenylalanine, and L-dopa to produce tyramine, 2-phenylethylamine, and dopamine, respectively^[1][2].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

9002-09-9

Solid

Off-white to light yellow

[Tyrosine decarboxylase, Microorganism]

4.1.1.25

≥0.2 U/mg soild

One Unit results in the decomposition of one micromole of tyrosine per minute at 37°C under the specified conditions

Room temperature in continental US; may vary elsewhere.

Please store the product under the recommended conditions in the Certificate of Analysis.

• [1]. Gatto V, et al. Tyrosine decarboxylase activity of Enterococcus mundtii: new insights into phenotypic and genetic aspects. Microb Biotechnol. 2016;9(6):801-813.  [Content Brief]

  [2]. Zhu H, et al. Crystal structure of tyrosine decarboxylase and identification of key residues involved in conformational swing and substrate binding. Sci Rep. 2016;6:27779. Published 2016 Jun 13.  [Content Brief]