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Histidine Decarboxylase
Histidine Decarboxylase (HDC) is an enzyme that is responsible for converting histamine from amino acid L-histidine. This enzyme belongs in the group II pyridoxal-5-phosphate (PLP)-dependent decarboxylase family. As the name suggested, this enzyme catalyzes the production of histamine by the removal of carboxylate group from the amino acid L-histidine whilst utilize pyridoxal phosphate as a cofactor. The mammalian Histamine decarboxylase is originated from HDC gene which encodes a 74kDa precursor polypeptide [1] [2]. However, the enzyme becomes active when its C-terminal is truncated into 54kDa during post-translation process [3] [4] [5] [6]
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General Information
Histidine Decarboxylase
Symbol: HDC [4e10]
Protein Bank Code: 4E1O
Gene Name: HDC gene
Organism: Homo sapiens
Length: 481 residues
Chains: A, B, C, D, E, F
Molecular Weight: 54314.8
Isoelectric Point: 5.4
Km: 0.1 mM
Vmax: 1880 nmol/min/mg
Structure
Implication
Histidine decarboxylase is responsible for the synthesis of histamine. Histamine is an important key factor for various physiological processes such as gastric acid secretion (3,4), immune response (1,2), cell growth (8-10), and neurotrasmission for appetite, memory, or circadian rhythm (5-7). As a result, any imbalance or distortion of the histamine metabolism can often contribute to a high probability for peptic ulcer, inflammation responses, schizophrenia, or tumor progression (5-7).
References
- ↑ Schwelberger, Hubert G. "Metabolism of Histamine." European Histamine Research Society Nov. 2013. Web. 29 Nov. 2013. http://www.ehrs.org.uk/schwelberger.pdf
- ↑ Komori H, Nitta Y, Ueno H, Higuchi Y. Structural study reveals Ser345 determines substrate specificity on human histidine decarboxylase. J Biol Chem. 2012 Jul 5. PMID:22767596 doi:10.1074/jbc.M112.381897
- ↑ Schwelberger, Hubert G. "Metabolism of Histamine." European Histamine Research Society Nov. 2013. Web. 29 Nov. 2013. http://www.ehrs.org.uk/schwelberger.pdf
- ↑ Taguchi Y, Watanabe T, Kubota H, Hayashi H, Wada H. Purification of histidine decarboxylase from the liver of fetal rats and its immunochemical and immunohistochemical characterization. J Biol Chem. 1984 Apr 25;259(8):5214-21. PMID:6425286
- ↑ Ohmori E, Fukui T, Imanishi N, Yatsunami K, Ichikawa A. Purification and characterization of l-histidine decarboxylase from mouse mastocytoma P-815 cells. J Biochem. 1990 Jun;107(6):834-9. PMID:2118138
- ↑ Komori H, Nitta Y, Ueno H, Higuchi Y. Structural study reveals Ser345 determines substrate specificity on human histidine decarboxylase. J Biol Chem. 2012 Jul 5. PMID:22767596 doi:10.1074/jbc.M112.381897
