first enzyme in poppy alkaloid biosynthesis, first biosynthetic step in the tetrahydroisoquinoline pathway, TyDC serves as a channel between the aromatic amino acids L-thyrosine and L-dopa and the biosynthesis of all of the opium poppy alkaloids
exclusive substrate specificity for L-amino acids with either indole or phenol side chains, but not both, inactive toward L-phenylalanine and L-tryptophan
TDC catalyzes the decarboxylation of tryptophan to tryptamine and 5-hydroxytryptophan to serotonin. Tryptophan is a good ligand showing the highest binding affinity. Tyrosine and dopa show the same binding affinity only slightly lower as tryptophan
TDC catalyzes the decarboxylation of tryptophan to tryptamine and 5-hydroxytryptophan to serotonin. Tryptophan is a good ligand showing the highest binding affinity. Tyrosine and dopa show the same binding affinity only slightly lower as tryptophan
first enzyme in poppy alkaloid biosynthesis, first biosynthetic step in the tetrahydroisoquinoline pathway, TyDC serves as a channel between the aromatic amino acids L-thyrosine and L-dopa and the biosynthesis of all of the opium poppy alkaloids
PLP, binding structure, overview. The cofactor is covalently attached to the epsilon-amino group of K321 to form an internal aldimine via a Schiff-base interaction. The protonated pyridine nitrogen of PLP forms a pair of salt bridges to the carboxyl group of D289. The PLP pyridine ring is anchored by the methyl group of A291 and the imidazole ring of H205. The O3 atom of the pyridine ring of PLP seems to interact with T264 adjacent water molecules. The phosphate moiety of PLP is stabilized by a number of interactions with T169, C170, N318 of one subunit, and R373 of the other subunit
recombinant TyDC5 expression pattern, not in poppy laticifers, about 15 members of the TyDC gene family show differences in developmental, tissue-specific and inducible gene expression
tyrosine decarboxylase (TyDC) is a member of aromatic amino acid decarboxylases (AAADs), which are a group of phylogenetically diverse enzymes grouped together based on their pyridoxal 5'-phosphate (PLP) dependence and sequence homology. Tyrosine decarboxylase (TyDC) is a type II pyridoxal 5'-phosphate decarboxylase that has a generally high sequence identity to other aromatic amino acid decarboxylases (AAADs)
structural basis of the substrate selectivity of enzyme TyDC9, crystal structure analysis, and molecular docking of tyrosine, dopa, tyrosine, tryptophan into the active site and simulation revealing the substrate binding sites and the residues required for conformational stability, active site analysis, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant tagged enzyme, hanging drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein in 25 mM HEPES, pH 7.0, and 0.04 mM pyridoxal 5'-phosphate, with 0.001 ml of reservoir solution containing 0.2 M NaOAc and 1 M NH4H2PO4, and equilibration against 0.45 ml of reservoir solution, X-ray diffraction structure determination and analysis at 3.1 A resolution
transgenic Nicotiana tabacum cv. Xanthi is engineered to constitutively express tobacco THT (EC 2.3.1.110). A T1 plant overexpressing THT is crossbred with T1 tobacco expressing opium poppy TYDC2 (EC 4.1.1.25), to produce a T2 line with elevated THT and TYDC activities compared with wild type plants