Literature summary for 4.1.1.28 extracted from

Ruiz-Perez, M.V.; Pino-Angeles, A.; Medina, M.A.; Sanchez-Jimenez, F.; Moya-Garcia, A.A.
Structural perspective on the direct inhibition mechanism of EGCG on mammalian histidine decarboxylase and DOPA decarboxylase (2012), J. Chem. Inf. Model., 52, 113-119.

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Sus scrofa

Crystallization (Comment)

Organism

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

Sus scrofa

Inhibitors

Inhibitors	Comment	Organism	Structure
epigallocatechin-3-gallate	direct inhibitory effect on both histidine decarboxylase and DOPA decarboxylase. Modeling of binding to the enzymes. 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	Sus scrofa

Organism

Organism	UniProt	Comment	Textmining
Sus scrofa	P80041	-	-

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Release 2023.1 (January 2023)