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Literature summary 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.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.22 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
4.1.1.28 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

EC Number Inhibitors Comment Organism Structure
4.1.1.22 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
4.1.1.28 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

EC Number Organism UniProt Comment Textmining
4.1.1.22 Rattus norvegicus
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4.1.1.28 Sus scrofa P80041
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