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Histidine decarboxylase

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Title: Histidine decarboxylase  
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Subject: Antihistamine, Histamine, Histidine, HDC, Pyruvate decarboxylase
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Histidine decarboxylase

Histidine decarboxylase
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols  ; MGC163399
External IDs GeneCards:
EC number
Species Human Mouse
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search
histidine decarboxylase
EC number
CAS number 9024-61-7
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO
Histidine carboxylase PI chain
structure of the d53,54n mutant of histidine decarboxylase at-170 c
Symbol HDC
Pfam PF02329
InterPro IPR003427
SCOP 1pya

Histidine decarboxylase (HDC) is the enzyme that catalyzes the reaction that produces histamine from histidine with the help of vitamin B6 as follows:[1][2][3]

Conversion of histidine to histamine by histidine decarboxylase

In humans, the histidine decarboxylase enzyme is encoded by the HDC gene.[4][5]


  • Function 1
  • Biosynthesis 2
  • Clinical significance 3
  • See also 4
  • References 5
  • Further reading 6
  • External links 7


The biogenic amine histamine is an important modulator of numerous physiologic processes, including neurotransmission, gastric acid secretion, and smooth muscle tone. The biosynthesis of histamine from histidine is catalyzed by the enzyme L-histidine decarboxylase. This homodimeric enzyme is a pyridoxal phosphate (PLP)-dependent decarboxylase and is highly specific for its histidine substrate.[4]


In bacteria, it is synthesised as a proenzyme, PI. Cleavage of the proenzyme PI chain yields two subunits, alpha and beta, which arrange as a hexamer, (alpha beta)6, by nonhydrolytic self-catalysis.[6]

Clinical significance

Known inhibitors of histidine decarboxylase : catechin, tritoqualine an atypical antihistaminic (Hypostamin©).

Mutations in the gene for this enzyme have been observed in one family with Tourette syndrome (TS) and are not thought to account for most cases of TS.[7]

See also


  1. ^ Epps HM (1945). "Studies on bacterial amino-acid decarboxylases: 4. l(-)-histidine decarboxylase from Cl. welchii Type A". Biochem. J. 39 (1): 42–6.  
  2. ^ Riley WD, Snell EE (October 1968). "Histidine decarboxylase of Lactobacillus 30a. IV. The presence of covalently bound pyruvate as the prosthetic group". Biochemistry 7 (10): 3520–8.  
  3. ^ Rosenthaler J, Guirard BM, Chang GW, Snell EE (July 1965). "Purification and properties of histidine decarboxylase from Lactobacillus 30a". Proc. Natl. Acad. Sci. U.S.A. 54 (1): 152–8.  
  4. ^ a b "Entrez Gene: histidine decarboxylase". 
  5. ^ Bruneau G, Nguyen VC, Gros F, Bernheim A, Thibault J (November 1992). "Preparation of a rat brain histidine decarboxylase (HDC) cDNA probe by PCR and assignment of the human HDC gene to chromosome 15". Hum. Genet. 90 (3): 235–8.  
  6. ^ Coton E, Rollan GC, Lonvaud-Funel A (1998). "Histidine carboxylase of Leuconostoc oenos 9204: purification, kinetic properties, cloning and nucleotide sequence of the hdc gene.". J Appl Microbiol 84 (2): 143–51.  
  7. ^ "Online Mendelian Inheritance in Man: histidine decarboxylase". 

Further reading

  • Need AC, Keefe RS, Ge D, et al. (2009). "Pharmacogenetics of antipsychotic response in the CATIE trial: a candidate gene analysis.". Eur. J. Hum. Genet. 17 (7): 946–57.  
  • Masini E, Fabbroni V, Giannini L, et al. (2005). "Histamine and histidine decarboxylase up-regulation in colorectal cancer: correlation with tumor stage.". Inflamm. Res. 54 Suppl 1: S80–1.  
  • Li Z, Liu J, Tang F, et al. (2008). "Expression of non-mast cell histidine decarboxylase in tumor-associated microvessels in human esophageal squamous cell carcinomas.". APMIS 116 (12): 1034–42.  
  • Szafranski K, Schindler S, Taudien S, et al. (2007). "Violating the splicing rules: TG dinucleotides function as alternative 3' splice sites in U2-dependent introns.". Genome Biol. 8 (8): R154.  
  • Ai W, Liu Y, Langlois M, Wang TC (2004). "Kruppel-like factor 4 (KLF4) represses histidine decarboxylase gene expression through an upstream Sp1 site and downstream gastrin responsive elements.". J. Biol. Chem. 279 (10): 8684–93.  
  • Raychowdhury R, Fleming JV, McLaughlin JT, et al. (2002). "Identification and characterization of a third gastrin response element (GAS-RE3) in the human histidine decarboxylase gene promoter.". Biochem. Biophys. Res. Commun. 297 (5): 1089–95.  
  • Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65.  
  • Sköldberg F, Portela-Gomes GM, Grimelius L, et al. (2003). "Histidine decarboxylase, a pyridoxal phosphate-dependent enzyme, is an autoantigen of gastric enterochromaffin-like cells.". J. Clin. Endocrinol. Metab. 88 (4): 1445–52.  
  • Brew O, Lakasing L, Sullivan M (2007). "Differential activity of histidine decarboxylase in normal and pre-eclamptic placentae.". Placenta 28 (5-6): 585–7.  
  • Zhang F, Xiong DH, Wang W, et al. (2006). "HDC gene polymorphisms are associated with age at natural menopause in Caucasian women.". Biochem. Biophys. Res. Commun. 348 (4): 1378–82.  
  • Tippens AS, Gruetter CA (2004). "Detection of histidine decarboxylase mRNA in human vascular smooth muscle and endothelial cells.". Inflamm. Res. 53 (6): 215–6.  
  • Siezen CL, Bont L, Hodemaekers HM, et al. (2009). "Genetic susceptibility to respiratory syncytial virus bronchiolitis in preterm children is associated with airway remodeling genes and innate immune genes.". Pediatr. Infect. Dis. J. 28 (4): 333–5.  
  • Morgan TK, Montgomery K, Mason V, et al. (2006). "Upregulation of histidine decarboxylase expression in superficial cortical nephrons during pregnancy in mice and women.". Kidney Int. 70 (2): 306–14.  
  • Papadopoulou N, Kalogeromitros D, Staurianeas NG, et al. (2005). "Corticotropin-releasing hormone receptor-1 and histidine decarboxylase expression in chronic urticaria.". J. Invest. Dermatol. 125 (5): 952–5.  
  • Janssen R, Bont L, Siezen CL, et al. (2007). "Genetic susceptibility to respiratory syncytial virus bronchiolitis is predominantly associated with innate immune genes.". J. Infect. Dis. 196 (6): 826–34.  
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903.  
  • Aichberger KJ, Mayerhofer M, Vales A, et al. (2006). "The CML-related oncoprotein BCR/ABL induces expression of histidine decarboxylase (HDC) and the synthesis of histamine in leukemic cells.". Blood 108 (10): 3538–47.  
  • Lee JK, Kim HT, Cho SM, et al. (2003). "Characterization of 458 single nucleotide polymorphisms of disease candidate genes in the Korean population.". J. Hum. Genet. 48 (5): 213–6.  
  • Jeong HJ, Moon PD, Kim SJ, et al. (2009). "Activation of hypoxia-inducible factor-1 regulates human histidine decarboxylase expression.". Cell. Mol. Life Sci. 66 (7): 1309–19.  

External links

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