Histidine ammonia-lyase (EC 4.3.1.3, histidase, histidinase) is an enzyme that in humans is encoded by the HALgene.[5][6] It converts histidine into ammonia and urocanic acid. Its systematic name is L-histidine ammonia-lyase (urocanate-forming).
Proposed autocatalytic formation of MIO cofactor in another enzyme, phenylalanine ammonia-lyase, from the tripeptide Ala-Ser-Gly by two water elimination steps.
Histidine ammonia-lyase is a cytosolic enzyme catalyzing the first reaction in histidine catabolism, the nonoxidative deamination of L-histidine to trans-urocanic acid.[5] The reaction is catalyzed by 3,5-dihydro-5-methyldiene-4H-imidazol-4-one (MIO), an electrophilic cofactor which is formed autocatalytically by cyclization of the protein backbone of the enzyme.[7]
^Suchi M, Sano H, Mizuno H, Wada Y (September 1995). "Molecular cloning and structural characterization of the human histidase gene (HAL)". Genomics. 29 (1): 98–104. doi:10.1006/geno.1995.1219. PMID 8530107.
^Schwede TF, Rétey J, Schulz GE (Apr 27, 1999). "Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile". Biochemistry. 38 (17): 5355–5361. doi:10.1021/bi982929q. PMID 10220322.
Further readingedit
Suchi M, Harada N, Wada Y, Takagi Y (1993). "Molecular cloning of a cDNA encoding human histidase". Biochim. Biophys. Acta. 1216 (2): 293–5. doi:10.1016/0167-4781(93)90157-9. PMID 7916645.
Davila S, Froeling FE, Tan A, et al. (2010). "New genetic associations detected in a host response study to hepatitis B vaccine". Genes Immun. 11 (3): 232–8. doi:10.1038/gene.2010.1. PMID 20237496. S2CID 11183658.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC528928. PMID 15489334.
Eckhart L, Schmidt M, Mildner M, et al. (2008). "Histidase expression in human epidermal keratinocytes: regulation by differentiation status and all-trans retinoic acid". J. Dermatol. Sci. 50 (3): 209–15. doi:10.1016/j.jdermsci.2007.12.009. PMID 18280705.
Welsh MM, Karagas MR, Applebaum KM, et al. (2008). "A role for ultraviolet radiation immunosuppression in non-melanoma skin cancer as evidenced by gene-environment interactions". Carcinogenesis. 29 (10): 1950–4. doi:10.1093/carcin/bgn160. PMC2556967. PMID 18641401.
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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. JSTOR 3074035. PMC139241. PMID 12477932.
Kawai Y, Moriyama A, Asai K, et al. (2005). "Molecular characterization of histidinemia: identification of four missense mutations in the histidase gene". Hum. Genet. 116 (5): 340–6. doi:10.1007/s00439-004-1232-5. PMID 15806399. S2CID 33960184.
Taylor RG, García-Heras J, Sadler SJ, et al. (1991). "Localization of histidase to human chromosome region 12q22→q24.1 and mouse chromosome region 10C2→D1". Cytogenet. Cell Genet. 56 (3–4): 178–81. doi:10.1159/000133082. PMID 2055114.
Alemán G, Ortíz V, Langley E, et al. (2005). "Regulation by glucagon of the rat histidase gene promoter in cultured rat hepatocytes and human hepatoblastoma cells". Am. J. Physiol. Endocrinol. Metab. 289 (1): E172–9. doi:10.1152/ajpendo.00584.2004. PMID 15741241.
External linksedit
Histidine+Ammonia-Lyase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
histidine, ammonia, lyase, histidase, histidinase, enzyme, that, humans, encoded, gene, converts, histidine, into, ammonia, urocanic, acid, systematic, name, histidine, ammonia, lyase, urocanate, forming, halidentifiersaliaseshal, hstd, histidine, ammonia, lya. Histidine ammonia lyase EC 4 3 1 3 histidase histidinase is an enzyme that in humans is encoded by the HAL gene 5 6 It converts histidine into ammonia and urocanic acid Its systematic name is L histidine ammonia lyase urocanate forming HALIdentifiersAliasesHAL HIS HSTD histidine ammonia lyase Histidine ammonia lyaseExternal IDsOMIM 609457 MGI 96010 HomoloGene 68229 GeneCards HALGene location Human Chr Chromosome 12 human 1 Band12q23 1Start95 972 662 bp 1 End95 996 365 bp 1 Gene location Mouse Chr Chromosome 10 mouse 2 Band10 C2 10 48 49 cMStart93 324 630 bp 2 End93 355 166 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inright lobe of liverhuman penisvulvabloodoocytemonocytesecondary oocyteskin of abdomenbone marrownippleTop expressed inleft lobe of liverlipskin of backcalvariabelly cordspermatidankle jointmorulagallbladderskin of abdomenMore reference expression dataBioGPSn aGene ontologyMolecular functioncatalytic activity lyase activity ammonia lyase activity histidine ammonia lyase activityCellular componentcytosol cytoplasmBiological processhistidine metabolic process histidine catabolic process to glutamate and formate histidine catabolic process to glutamate and formamide histidine catabolic processSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez303415109EnsemblENSG00000084110ENSMUSG00000020017UniProtP42357P35492RefSeq mRNA NM 001258333NM 001258334NM 002108NM 010401RefSeq protein NP 001245262NP 001245263NP 002099NP 034531Location UCSC Chr 12 95 97 96 MbChr 10 93 32 93 36 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse histidine ammonia lyaseHistidine ammonia lyase homotetramer Pseudomonas putidaIdentifiersEC no 4 3 1 3CAS no 9013 75 6DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumGene OntologyAmiGO QuickGOSearchPMCarticlesPubMedarticlesNCBIproteins Contents 1 Function 2 Pathology 3 See also 4 References 5 Further reading 6 External linksFunction edit nbsp Proposed autocatalytic formation of MIO cofactor in another enzyme phenylalanine ammonia lyase from the tripeptide Ala Ser Gly by two water elimination steps Histidine ammonia lyase is a cytosolic enzyme catalyzing the first reaction in histidine catabolism the nonoxidative deamination of L histidine to trans urocanic acid 5 The reaction is catalyzed by 3 5 dihydro 5 methyldiene 4H imidazol 4 one MIO an electrophilic cofactor which is formed autocatalytically by cyclization of the protein backbone of the enzyme 7 Pathology editMutations in the gene for histidase are associated with histidinemia and urocanic aciduria See also editPhenylalanine ammonia lyase another enzyme that contains the MIO cofactorReferences edit a b c GRCh38 Ensembl release 89 ENSG00000084110 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000020017 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine a b Entrez Gene histidine ammonia lyase Suchi M Sano H Mizuno H Wada Y September 1995 Molecular cloning and structural characterization of the human histidase gene HAL Genomics 29 1 98 104 doi 10 1006 geno 1995 1219 PMID 8530107 Schwede TF Retey J Schulz GE Apr 27 1999 Crystal structure of histidine ammonia lyase revealing a novel polypeptide modification as the catalytic electrophile Biochemistry 38 17 5355 5361 doi 10 1021 bi982929q PMID 10220322 Further reading editSuchi M Harada N Wada Y Takagi Y 1993 Molecular cloning of a cDNA encoding human histidase Biochim Biophys Acta 1216 2 293 5 doi 10 1016 0167 4781 93 90157 9 PMID 7916645 Davila S Froeling FE Tan A et al 2010 New genetic associations detected in a host response study to hepatitis B vaccine Genes Immun 11 3 232 8 doi 10 1038 gene 2010 1 PMID 20237496 S2CID 11183658 Gerhard DS Wagner L Feingold EA et al 2004 The status quality and expansion of the NIH full length cDNA project the Mammalian Gene Collection MGC Genome Res 14 10B 2121 7 doi 10 1101 gr 2596504 PMC 528928 PMID 15489334 Eckhart L Schmidt M Mildner M et al 2008 Histidase expression in human epidermal keratinocytes regulation by differentiation status and all trans retinoic acid J Dermatol Sci 50 3 209 15 doi 10 1016 j jdermsci 2007 12 009 PMID 18280705 Welsh MM Karagas MR Applebaum KM et al 2008 A role for ultraviolet radiation immunosuppression in non melanoma skin cancer as evidenced by gene environment interactions Carcinogenesis 29 10 1950 4 doi 10 1093 carcin bgn160 PMC 2556967 PMID 18641401 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 Bibcode 2002PNAS 9916899M doi 10 1073 pnas 242603899 JSTOR 3074035 PMC 139241 PMID 12477932 Kawai Y Moriyama A Asai K et al 2005 Molecular characterization of histidinemia identification of four missense mutations in the histidase gene Hum Genet 116 5 340 6 doi 10 1007 s00439 004 1232 5 PMID 15806399 S2CID 33960184 Taylor RG Garcia Heras J Sadler SJ et al 1991 Localization of histidase to human chromosome region 12q22 q24 1 and mouse chromosome region 10C2 D1 Cytogenet Cell Genet 56 3 4 178 81 doi 10 1159 000133082 PMID 2055114 Aleman G Ortiz V Langley E et al 2005 Regulation by glucagon of the rat histidase gene promoter in cultured rat hepatocytes and human hepatoblastoma cells Am J Physiol Endocrinol Metab 289 1 E172 9 doi 10 1152 ajpendo 00584 2004 PMID 15741241 External links editHistidine Ammonia Lyase 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 Portal nbsp Biology This lyase article is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title Histidine ammonia 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