Structural highlights
Function
TYRDC_LEVBR Catalyzes the decarboxylation of L-tyrosine to produce tyramine (PubMed:24211777, PubMed:27292129). Cannot use other aromatic L-amino acids as substrates like L-phenylalanine, L-tryptophan and L-glutamate (PubMed:24211777).[1] [2] Is also able to decarboxylate the Parkinson's disease medication levodopa (L-dopa) to dopamine in vitro.[3] [4]
References
- ↑ Zhang K, Ni Y. Tyrosine decarboxylase from Lactobacillus brevis: soluble expression and characterization. Protein Expr Purif. 2014 Feb;94:33-9. PMID:24211777 doi:10.1016/j.pep.2013.10.018
- ↑ Zhu H, Xu G, Zhang K, Kong X, Han R, Zhou J, Ni Y. Crystal structure of tyrosine decarboxylase and identification of key residues involved in conformational swing and substrate binding. Sci Rep. 2016 Jun 13;6:27779. doi: 10.1038/srep27779. PMID:27292129 doi:https://dx.doi.org/10.1038/srep27779
- ↑ Zhang K, Ni Y. Tyrosine decarboxylase from Lactobacillus brevis: soluble expression and characterization. Protein Expr Purif. 2014 Feb;94:33-9. PMID:24211777 doi:10.1016/j.pep.2013.10.018
- ↑ Zhu H, Xu G, Zhang K, Kong X, Han R, Zhou J, Ni Y. Crystal structure of tyrosine decarboxylase and identification of key residues involved in conformational swing and substrate binding. Sci Rep. 2016 Jun 13;6:27779. doi: 10.1038/srep27779. PMID:27292129 doi:https://dx.doi.org/10.1038/srep27779
