Characterization and expression of the complementary DNA encoding rat histidine decarboxylase.

Journal Article (Journal Article)

Histamine is a neurotransmitter in the central nervous system and an important modulator of gastric acid secretion, vasomotor control, inflammation, and allergic reactions. In biological systems the formation of histamine from its precursor histidine is catalyzed by the enzyme L-histidine decarboxylase (HDC; L-histidine carboxy-lyase, EC We have cloned HDC-encoding cDNA from a fetal rat liver cDNA library (phage lambda gt11) have deduced the amino acid sequence from the nucleotide sequence. The clone was proven to be HDC cDNA by expression of active recombinant enzyme in COS cells and by chromosomal mapping. The cDNA encodes a protein of Mr 73,450 (655 amino acid residues). The discrepancy between this molecular weight and the size of the purified fetal liver protein subunits [Taguchi, Y., Watanabe, T., Kubota, H., Hayashi, H. & Wada, H. (1984) J. Biol. Chem. 259, 5214-5221] (Mr = 54,000) suggests that HDC may be posttranslationally processed. The 469 amino acid residues from the amino-terminal portion of the protein share 50% identity with rat and Drosophila L-dopa decarboxylases and much less homology with other characterized amino acid decarboxylases.

Full Text

Duke Authors

Cited Authors

  • Joseph, DR; Sullivan, PM; Wang, YM; Kozak, C; Fenstermacher, DA; Behrendsen, ME; Zahnow, CA

Published Date

  • January 1990

Published In

Volume / Issue

  • 87 / 2

Start / End Page

  • 733 - 737

PubMed ID

  • 2300558

Pubmed Central ID

  • PMC53340

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.87.2.733


  • eng

Conference Location

  • United States