Histidine decarboxylase

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Histidine decarboxylase
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols HDC ; MGC163399
External IDs OMIM142704 MGI96062 HomoloGene20490 IUPHAR: 1274 GeneCards: HDC Gene
EC number
Species Human Mouse
Entrez 3067 15186
Ensembl ENSG00000140287 ENSMUSG00000027360
UniProt P19113 P23738
RefSeq (mRNA) NM_001306146 NM_008230
RefSeq (protein) NP_001293075 NP_032256
Location (UCSC) Chr 15:
50.24 – 50.27 Mb
Chr 2:
126.59 – 126.62 Mb
PubMed search [1] [2]
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
PDB 1ibt EBI.jpg
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]


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[edit]

Known inhibitors of histidine decarboxylase: catechin, tritoqualine an atypical antihistamine.

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[edit]


  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. PMC 1258146. PMID 16747851. 
  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. doi:10.1021/bi00850a029. PMID 5681461. 
  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. doi:10.1073/pnas.54.1.152. PMC 285813. PMID 5216347. 
  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. doi:10.1007/bf00220068. PMID 1487235. 
  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. doi:10.1046/j.1365-2672.1998.00271.x. PMID 9633629. 
  7. ^ "Online Mendelian Inheritance in Man: histidine decarboxylase". 

Further reading[edit]

External links[edit]

This article incorporates text from the United States National Library of Medicine, which is in the public domain.