Literature summary for 4.1.1.28 extracted from

Chakrabarty, K.; Gupta, S.N.; Das, G.K.; Roy, S.
Theoretical studies on the pyridoxal-5-phosphate dependent enzyme dopa decarboxylase: effect of Thr 246 residue on the co-factor-enzyme binding and reaction mechanism (2012), Indian J. Biochem. Biophys., 49, 155-164.

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Sus scrofa

Crystallization (Comment)

Organism

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

Sus scrofa

Organism

Organism	UniProt	Comment	Textmining
Sus scrofa	P80041	-	-

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Release 2023.1 (January 2023)