Histidine decarboxylase

Histidine decarboxylase
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsHDC ; MGC163399
External IDsOMIM: 142704 MGI: 96062 HomoloGene: 20490 IUPHAR: 1274 GeneCards: HDC Gene
EC number4.1.1.22
Orthologs
SpeciesHumanMouse
Entrez306715186
EnsemblENSG00000140287ENSMUSG00000027360
UniProtP19113P23738
RefSeq (mRNA)NM_002112NM_008230
RefSeq (protein)NP_002103NP_032256
Location (UCSC)Chr 15:
50.53 – 50.56 Mb
Chr 2:
126.59 – 126.62 Mb
PubMed search
histidine decarboxylase
Identifiers
EC number 4.1.1.22
CAS number 9024-61-7
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
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
Identifiers
Symbol HDC
Pfam PF02329
InterPro IPR003427
SCOP 1pya
SUPERFAMILY 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

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]

Biosynthesis

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 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

References

  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. 4.0 4.1 "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

External links

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