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4.1.1.28: aromatic-L-amino-acid decarboxylase

This is an abbreviated version!
For detailed information about aromatic-L-amino-acid decarboxylase, go to the full flat file.

Word Map on EC 4.1.1.28

Reaction

5-hydroxy-L-tryptophan
=
5-hydroxytryptamine
+
CO2

Synonyms

3,4-dihydroxyphenylalanine carboxylase, 3,4-Dihydroxyphenylalanine decarboxylase, 5-Hydroxy-L-tryptophan decarboxylase, 5-Hydroxytryptophan decarboxylase, 5-hydroxytryptophan hydroxylase, 5HTP decarboxylase, AAAC, AAAD, AACD, AADC, AADC1A, AADC1B, AADC393, AADC438, AADC486, Alt-DDC, aromatic acid acid decarboxylase, Aromatic amino acid decarboxylase, aromatic amino acid decarboxylase 1A, aromatic amino acid decarboxylase 1B, Aromatic L-amino acid decarboxylase, aromatic L-aminoacid decarboxylase, aromatic-L-amino-acid decarboxylase, CrTDC, DDC, Decarboxylase, aromatic amino acid, Di-ADC, Dihydroxyphenylalanine-5-hydroxytryptophan decarboxylase, DOPA DC, dopa decarboxilase, DOPA decarboxylase, DOPA-5-hydroxytryptophan decarboxylase, DOPA/5HTP decarboxylase, dopamine decarboxylase, EC 4.1.1.26, EC 4.1.1.27, HsDDC, Hydroxytryptophan decarboxylase, L-3,4-Dihydroxyphenylalanine decarboxylase, L-5-Hydroxytryptophan decarboxylase, L-amino acid decarboxylase, L-amino-acid decarboxylase, L-Aromatic amino acid decarboxylase, L-aromatic aminoacid decarboxylase, L-DOPA decarboxylase, L-Tryptophan decarboxylase, neural-type DDC, non-neural DDC, PP_2552, TDC, TDC2, Tenebrio Dopa decarboxylase, Trp decarboxylase, Tryptophan decarboxylase, tryptophan decarboxylase-1, tryptophan decarboxylase-2, TYDC, Tydc9, Tyrosine/Dopa decarboxylase

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.28 aromatic-L-amino-acid decarboxylase

Crystallization

Crystallization on EC 4.1.1.28 - aromatic-L-amino-acid decarboxylase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apoenzyme, to 2.9 A resolution. The apoenzyme exists in an unexpected open conformation. Compared to the pig kidney holoenzyme, the dimer subunits move 20 A apart and the two active sites become solvent exposed. Complete achievement of the closed conformation of the dimer is not essential for Schiff base formation and pyridoxal 5'-phosphate binding to the intermediate monomer is able to induce rearrangement of loop1. Covalent binding of the cofactor can only be achieved after an initial rearrangement towards the closed conformation
-
Micrococcus percitreus
-
density functional theory and real-time dynamics studies. In the crystal structure, residue Asp 271 interacts with the pyridine nitrogen atom of pyridoxal 5'-phosphate through H-bonding in both native and substrate-bound enzyme. Residue Thr 246 is in close proximity to the oxygen atom of 3-OH of the pyridoxal 5'-phosphate pyridine ring only in substrate-bound enzyme. In the ligand-free enzyme, this distance is not favorable for hydrogen bonding
modeling of complex with inhibitor epigallocatechin-3-gallate. Epigallocatechin-3-gallate does not affect the quaternary structure of the enzyme and remains stable in the active site throughout the entire trajectory. After 700 ps of simulation, epigallocatechin-3-gallate moves deeper into the active site. While adopting this conformation, epigallocatechin-3-gallate actually fills the binding pocket and blocks its entrance pathway