Mammalian histidine decarboxylase: from structure to function

Histamine is a multifunctional biogenic amine with relevant roles in intercellular communication, inflammatory processes and highly prevalent pathologies. Histamine biosynthesis depends on a single decarboxylation step, carried out by a PLP‐dependent histidine decarboxylase activity (EC 4.1.1.22), a...

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Bibliographic Details
Published in:BioEssays 2005-01, Vol.27 (1), p.57-63
Main Authors: Moya‐Garcia, Aurelio A., Medina, Miguel Ángel, Sánchez‐Jiménez, Francisca
Format: Article
Language:English
Subjects:
Animals
Histamine - chemistry
Histidine Decarboxylase - chemistry
Humans
Models, Biological
Models, Chemical
Models, Molecular
Peptides - chemistry
Protein Conformation
Rats
Structure-Activity Relationship
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Summary:Histamine is a multifunctional biogenic amine with relevant roles in intercellular communication, inflammatory processes and highly prevalent pathologies. Histamine biosynthesis depends on a single decarboxylation step, carried out by a PLP‐dependent histidine decarboxylase activity (EC 4.1.1.22), an enzyme that still remains to be fully characterized. Nevertheless, during the last few years, important advances have been made in this field, including the generation and validation of the first three‐dimensional model of the enzyme, which allows us to revisit previous results and conclusions. This essay provides a comprehensive review of the current knowledge of the structural and functional characteristics of mammalian histidine decarboxylase. BioEssays 27:57–63, 2005. © 2004 Wiley Periodicals, Inc.
ISSN:0265-9247
1521-1878
DOI:10.1002/bies.20174