Summary: Histidine carboxylase PI chain
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Histidine decarboxylase Edit Wikipedia article
| histidine decarboxylase | |||||||||
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| 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 | ||||||||
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| Histidine carboxylase PI chain | |||||||||
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| structure of the d53,54n mutant of histidine decarboxylase at-170 c | |||||||||
| Identifiers | |||||||||
| Symbol | HDC | ||||||||
| Pfam | PF02329 | ||||||||
| InterPro | IPR003427 | ||||||||
| SCOP | 1pya | ||||||||
| SUPERFAMILY | 1pya | ||||||||
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| Histidine decarboxylase | |||||||||||||
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| Identifiers | |||||||||||||
| Symbols | HDC; MGC163399 | ||||||||||||
| External IDs | OMIM: 142704 MGI: 96062 HomoloGene: 20490 GeneCards: HDC Gene | ||||||||||||
| EC number | 4.1.1.22 | ||||||||||||
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| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 3067 | 15186 | |||||||||||
| Ensembl | ENSG00000140287 | ENSMUSG00000027360 | |||||||||||
| UniProt | P19113 | P23738 | |||||||||||
| RefSeq (mRNA) | NM_002112 | NM_008230 | |||||||||||
| RefSeq (protein) | NP_002103 | NP_032256 | |||||||||||
| Location (UCSC) | Chr 15: 50.53 â 50.56 Mb |
Chr 2: 126.59 â 126.62 Mb |
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| 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]
Known inhibitors of histidine decarboxylase : catechin, tritoqualine an atypical antihistaminic (Hypostamin©).
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]
Contents |
[edit] See also
[edit] References
- ^ Epps HM (1945). "Studies on bacterial amino-acid decarboxylases: 4. l(-)-histidine decarboxylase from Cl. welchii Type A". Biochem. J. 39 (1): 42â6. PMC 1258146. PMID 16747851. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1258146/.
- ^ 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): 3520â8. 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): 152â8. doi:10.1073/pnas.54.1.152. PMC 285813. PMID 5216347. //www.ncbi.nlm.nih.gov/pmc/articles/PMC285813/.
- ^ a b "Entrez Gene: histidine decarboxylase". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3067.
- ^ 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): 235â8. PMID 1487235.
- ^ "Online Mendelian Inheritance in Man: histidine decarboxylase". http://www.ncbi.nlm.nih.gov/omim/142704.
- ^ 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): 143â51. PMID 9633629.
[edit] 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): 946â57. doi:10.1038/ejhg.2008.264. PMC 2986499. PMID 19156168. //www.ncbi.nlm.nih.gov/pmc/articles/PMC2986499/.
- 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.
- 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): 1034â42. doi:10.1111/j.1600-0463.2008.01048.x. PMID 19133005.
- 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. //www.ncbi.nlm.nih.gov/pmc/articles/PMC2374985/.
- 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): 8684â93. doi:10.1074/jbc.M308278200. PMID 14670968.
- 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): 1089â95. doi:10.1016/S0006-291X(02)02345-8. PMID 12372397.
- 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): 55â65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1356129/.
- 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): 1445â52. doi:10.1210/jc.2002-021761. PMID 12679420.
- Brew O, Lakasing L, Sullivan M. "Differential activity of histidine decarboxylase in normal and pre-eclamptic placentae.". Placenta 28 (5-6): 585â7. doi:10.1016/j.placenta.2006.05.003. PMID 16822545.
- 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): 1378â82. doi:10.1016/j.bbrc.2006.08.008. PMID 16919600.
- Tippens AS, Gruetter CA (2004). "Detection of histidine decarboxylase mRNA in human vascular smooth muscle and endothelial cells.". Inflamm. Res. 53 (6): 215â6. 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): 333â5. doi:10.1097/INF.0b013e31818e2aa9. PMID 19258923.
- 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): 306â14. doi:10.1038/sj.ki.5001553. PMID 16760908.
- 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): 952â5. doi:10.1111/j.0022-202X.2005.23913.x. PMID 16297195.
- 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): 826â34. doi:10.1086/520886. PMID 17703412.
- 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): 16899â903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. //www.ncbi.nlm.nih.gov/pmc/articles/PMC139241/.
- 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): 3538â47. doi:10.1182/blood-2005-12-028456. PMID 16849647.
- 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): 213â6. doi:10.1007/s10038-003-0011-9. PMID 12768436.
- 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): 1309â19. doi:10.1007/s00018-009-9001-1. PMID 19266161.
[edit] External links
- Histidine Decarboxylase at the US 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.
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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Histidine carboxylase PI chain Provide feedback
Histidine carboxylase catalyses the formation of histamine from histidine. Cleavage of the proenzyme PI chain yields two subunits, alpha and beta, which arrange as a hexamer (alpha beta)6.
Literature references
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Coton E, Rollan GC, Lonvaud-Funel A; , J Appl Microbiol 1998;84:143-151.: Histidine carboxylase of Leuconostoc oenos 9204: purification, kinetic properties, cloning and nucleotide sequence of the hdc gene. PUBMED:9633629 EPMC:9633629
External database links
| PANDIT: | PF02329 |
| Pseudofam: | PF02329 |
| SCOP: | 1pya |
| SYSTERS: | HDC |
This tab holds annotation information from the InterPro database.
InterPro entry IPR003427
Histidine decarboxylase (EC) catalyses the formation of histamine from histidine [PUBMED:11243783]. It requires a pyruvoyl group for its activity. Cleavage of the proenzyme PI chain yields two subunits, alpha and beta, which arrange as a hexamer (alpha beta) 6 by nonhydrolytic self-catalysis.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Molecular function | histidine decarboxylase activity (GO:0004398) |
| Biological process | histidine metabolic process (GO:0006547) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
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| RP15 (4) |
RP35 (7) |
RP55 (8) |
RP75 (9) |
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| PP/heatmap | 1 | |||||||
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| Seed (4) |
Full (71) |
Representative proteomes | NCBI (58) |
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| RP15 (4) |
RP35 (7) |
RP55 (8) |
RP75 (9) |
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
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Trees
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Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Pfam-B_19599 (release 5.2) |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Mian N, Bateman A |
| Number in seed: | 4 |
| Number in full: | 71 |
| Average length of the domain: | 262.60 aa |
| Average identity of full alignment: | 46 % |
| Average coverage of the sequence by the domain: | 94.92 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 306 | ||||||||||||
| Family (HMM) version: | 11 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the HDC domain has been found. There are 34 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence