Mammalian histidine decarboxylase: from structure to function.

Aurelio A Moya-Garcia; Miguel Angel Medina; Francisca Sánchez-Jiménez

doi:10.1002/bies.20174

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Mammalian histidine decarboxylase: from structure to function.

Aurelio A Moya-Garcia·Miguel Angel Medina·Francisca Sánchez-Jiménez

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Abstract

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.

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Animals Histamine Histidine Decarboxylase Humans Models, Biological Models, Chemical Models, Molecular Peptides Protein Conformation Rats Structure-Activity Relationship Journal Article Research Support, Non-U.S. Gov't Review

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Aurelio A Moya-Garcia, Miguel Angel Medina, Francisca Sánchez-Jiménez. 2005. Mammalian histidine decarboxylase: from structure to function.. https://doi.org/10.1002/bies.20174

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