Histidine decarboxylase

histidine decarboxylase
Conversion of histidine to histamine by 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
Histidine decarboxylase
Identifiers
Symbols HDC; MGC163399
External IDs OMIM142704 MGI96062 HomoloGene20490 GeneCards: HDC Gene
EC number 4.1.1.22
Orthologs
Species Human Mouse
Entrez 3067 15186
Ensembl ENSG00000140287 ENSMUSG00000027360
UniProt P19113 P23738
RefSeq (mRNA) NM_002112 NM_008230.5
RefSeq (protein) NP_002103 NP_032256.3
Location (UCSC) Chr 15:
50.53 – 50.56 Mb
Chr 2:
126.42 – 126.45 Mb
PubMed search [1] [2]

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]

C6H9N3O2C5H9N3 + CO2

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]

Some mutations in the gene for this enzyme can cause symptoms of Tourette syndrome; however, these mutations have only been observed in one family and are not thought to account for most cases of Tourette syndrome.[6]

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.[7]

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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1258146. 
  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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=285813. 
  4. ^ a b "Entrez Gene: histidine decarboxylase". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3067. 
  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. PMID 1487235. 
  6. ^ "Online Mendelian Inheritance in Man: histidine decarboxylase". http://www.ncbi.nlm.nih.gov/omim/142704. 
  7. ^ 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. PMID 9633629. 

Further reading

External links

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