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Structural features of mammalian histidine decarboxylase reveal the basis for specific inhibition
Author(s) -
MoyaGarcía AA,
PinoÁngeles A,
GilRedondo R,
Morreale A,
SánchezJiménez F
Publication year - 2009
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/j.1476-5381.2009.00219.x
Subject(s) - histidine decarboxylase , histidine , histamine , enzyme , biochemistry , computational biology , carboxy lyases , chemistry , biology , pharmacology
For a long time the structural and molecular features of mammalian histidine decarboxylase (EC 4.1.1.22), the enzyme that produces histamine, have evaded characterization. We overcome the experimental problems for the study of this enzyme by using a computer‐based modelling and simulation approach, and have now the conditions to use histidine decarboxylase as a target in histamine pharmacology. In this review, we present the recent (last 5 years) advances in the structure–function relationship of histidine decarboxylase and the strategy for the discovery of new drugs.