Literature summary for 4.1.1.22 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. The presence of epigallocatechin-3-gallate contiguous to the active site entrance leads to the movement of several residues in the active site. Epigallocatechin-3-gallate occludes the entrance channel to the enzyme active site and establishes new interactions with residues in the active site. These residues turn outward when the active site collapses	Rattus norvegicus

Crystallization (Comment)

Organism

modeling of complex with inhibitor epigallocatechin-3-gallate. The presence of epigallocatechin-3-gallate contiguous to the active site entrance leads to the movement of several residues in the active site. Epigallocatechin-3-gallate occludes the entrance channel to the enzyme active site and establishes new interactions with residues in the active site. These residues turn outward when the active site collapses

Rattus norvegicus

Inhibitors

Inhibitors	Comment	Organism	Structure
epigallocatechin-3-gallate	direct inhibitory effect on both histidine decarboxylase and DOPA decarboxylase. Modeling of binding to the enzymes. The presence of epigallocatechin-3-gallate contiguous to the active site entrance leads to the movement of several residues in the active site. Epigallocatechin-3-gallate occludes the entrance channel to the enzyme active site and establishes new interactions with residues in the active site. These residues turn outward when the active site collapses. After docking of epigallocatechin-3-gallate, neither histidine nor the inhibitors histidine methyl ester and alpha-fluoromethyl histidine are able to bind to the enzyme	Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

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Release 2023.1 (January 2023)