Histidine decarboxylase
| histidine decarboxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.1.1.22 | ||||||||
| CAS no. | 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 / QuickGO | ||||||||
| |||||||||
| Histidine carboxylase PI chain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 structure of the d53,54n mutant of histidine decarboxylase at-170 c | |||||||||
| Identifiers | |||||||||
| Symbol | HDC | ||||||||
| Pfam | PF02329 | ||||||||
| InterPro | IPR003427 | ||||||||
| SCOP2 | 1pya / SCOPe / SUPFAM | ||||||||
| |||||||||
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]
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 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
References
- ^ 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.
- ^ 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.
- ^ 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) - ^ a b "Entrez Gene: histidine decarboxylase".
- ^ 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) - ^ 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) - ^ "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. doi:10.1038/ejhg.2008.264. PMC 2986499. PMID 19156168.
{{cite journal}}: Explicit use of et al. in:|author=(help)CS1 maint: multiple names: authors list (link) - 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. doi:10.1007/s00011-004-0437-3. PMID 15928846.
{{cite journal}}: Explicit use of et al. in:|author=(help)CS1 maint: multiple names: authors list (link) - 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. doi:10.1111/j.1600-0463.2008.01048.x. PMID 19133005.
{{cite journal}}: Explicit use of et al. in:|author=(help)CS1 maint: multiple names: authors list (link) - 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. doi:10.1186/gb-2007-8-8-r154. PMC 2374985. PMID 17672918.
{{cite journal}}: Explicit use of et al. in:|author=(help)CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link) - 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. doi:10.1074/jbc.M308278200. PMID 14670968.
{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link) - 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. doi:10.1016/S0006-291X(02)02345-8. PMID 12372397.
{{cite journal}}: Explicit use of et al. in:|author=(help)CS1 maint: multiple names: authors list (link) - 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. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
{{cite journal}}: Explicit use of et al. in:|author=(help)CS1 maint: multiple names: authors list (link) - 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. doi:10.1210/jc.2002-021761. PMID 12679420.
{{cite journal}}: Explicit use of et al. in:|author=(help)CS1 maint: multiple names: authors list (link) - Brew O, Lakasing L, Sullivan M (2007). "Differential activity of histidine decarboxylase in normal and pre-eclamptic placentae". Placenta. 28 (5–6): 585–7. doi:10.1016/j.placenta.2006.05.003. PMID 16822545.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - 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. doi:10.1016/j.bbrc.2006.08.008. PMC 1803761. PMID 16919600.
{{cite journal}}: Explicit use of et al. in:|author=(help)CS1 maint: multiple names: authors list (link) - Tippens AS, Gruetter CA (2004). "Detection of histidine decarboxylase mRNA in human vascular smooth muscle and endothelial cells". Inflamm. Res. 53 (6): 215–6. doi:10.1007/s00011-004-1252-6. PMID 15167966.
- 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. doi:10.1097/INF.0b013e31818e2aa9. PMID 19258923.
{{cite journal}}: Explicit use of et al. in:|author=(help)CS1 maint: multiple names: authors list (link) - 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. doi:10.1038/sj.ki.5001553. PMID 16760908.
{{cite journal}}: Explicit use of et al. in:|author=(help)CS1 maint: multiple names: authors list (link) - 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. doi:10.1111/j.0022-202X.2005.23913.x. PMID 16297195.
{{cite journal}}: Explicit use of et al. in:|author=(help)CS1 maint: multiple names: authors list (link) - 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. doi:10.1086/520886. PMID 17703412.
{{cite journal}}: Explicit use of et al. in:|author=(help)CS1 maint: multiple names: authors list (link) - 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
{{cite journal}}: Explicit use of et al. in:|author=(help)CS1 maint: multiple names: authors list (link) - 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. doi:10.1182/blood-2005-12-028456. PMID 16849647.
{{cite journal}}: Explicit use of et al. in:|author=(help)CS1 maint: multiple names: authors list (link) - 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. doi:10.1007/s10038-003-0011-9. PMID 12768436.
{{cite journal}}: Explicit use of et al. in:|author=(help)CS1 maint: multiple names: authors list (link) - 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. doi:10.1007/s00018-009-9001-1. PMID 19266161.
{{cite journal}}: Explicit use of et al. in:|author=(help)CS1 maint: multiple names: authors list (link)
External links
- Histidine+Decarboxylase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the United States National Library of Medicine, which is in the public domain.