Histidine decarboxylase

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HDC
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesHDC, entrez:3067, Histidine decarboxylase
External IDsOMIM: 142704 MGI: 96062 HomoloGene: 20490 GeneCards: HDC
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001306146
NM_002112

NM_008230

RefSeq (protein)

NP_001293075
NP_002103

NP_032256

Location (UCSC)Chr 15: 50.24 – 50.27 MbChr 2: 126.44 – 126.46 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse
histidine decarboxylase
Identifiers
EC no.4.1.1.22
CAS no.9024-61-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
Histidine carboxylase PI chain
structure of the d53,54n mutant of histidine decarboxylase at-170 c
Identifiers
SymbolHDC
PfamPF02329
InterProIPR003427
SCOP21pya / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Histidine decarboxylase (HDC) is the enzyme that catalyzes the reaction that produces histamine from histidine with the help of vitamin B6 as follows:[5][6][7]

Conversion of histidine to histamine by histidine decarboxylase

In humans, the histidine decarboxylase enzyme is encoded by the HDC gene.[8][9]

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.[8]

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.[10]

Clinical significance

Inhibitors of histidine decarboxylase can be used as atypical antihistamines. (See Tritoqualine)

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.[11]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000140287Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027360Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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.
  6. ^ 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.
  7. ^ 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.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  8. ^ a b "Entrez Gene: histidine decarboxylase".
  9. ^ 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.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  10. ^ 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.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  11. ^ "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.