Literature summary for 4.1.1.25 extracted from

Guan, H.; Song, S.; Robinson, H.; Liang, J.; Ding, H.; Li, J.; Han, Q.
Structural basis of the substrate specificity and enzyme catalysis of a Papaver somniferum tyrosine decarboxylase (2017), Front. Mol. Biosci., 4, 5-5 .

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Cloned(Commentary)

Cloned (Comment)	Organism
gene tdc, recombinant expression of tagged enzyme	Papaver somniferum

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Papaver somniferum

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-Tyrosine	Papaver somniferum	-	Tyramine + CO2	-	?
additional information	Papaver somniferum	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	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Papaver somniferum	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant tagged enzyme by affinity and anion exchange chromatography, and gel filtration	Papaver somniferum

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-Tyrosine	-	Papaver somniferum	Tyramine + CO2	-	?
additional information	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	Papaver somniferum	?	-	?

Subunits

Subunits	Comment	Organism
dimer	-	Papaver somniferum

Synonyms

Synonyms	Comment	Organism
TYDC	-	Papaver somniferum
Tydc9	-	Papaver somniferum

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	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	Papaver somniferum

General Information

General Information	Comment	Organism
evolution	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)	Papaver somniferum
additional information	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	Papaver somniferum

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Release 2023.1 (January 2023)