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).
Function
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
Mutations in the gene for histidase are associated with histidinemia and urocanic aciduria.
See also
References
- ^ 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 T, Rétey J, Schulz G (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
- Suchi M, Harada N, Wada Y, Takagi Y (Nov 1993). "Molecular cloning of a cDNA encoding human histidase". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1216 (2): 293–295. doi:10.1016/0167-4781(93)90157-9. PMID 7916645.
- Davila S, Froeling FE, Tan A, Bonnard C, Boland GJ, Snippe H, et al. (Apr 2010). "New genetic associations detected in a host response study to hepatitis B vaccine". Genes and Immunity. 11 (3): 232–238. doi:10.1038/gene.2010.1. PMID 20237496. S2CID 11183658.
- Eckhart L, Schmidt M, Mildner M, Mlitz V, Abtin A, Ballaun C, et al. (Jun 2008). "Histidase expression in human epidermal keratinocytes: regulation by differentiation status and all-trans retinoic acid". Journal of Dermatological Science. 50 (3): 209–215. doi:10.1016/j.jdermsci.2007.12.009. PMID 18280705.
- Welsh MM, Karagas MR, Applebaum KM, Spencer SK, Perry AE, Nelson HH (Oct 2008). "A role for ultraviolet radiation immunosuppression in non-melanoma skin cancer as evidenced by gene-environment interactions". Carcinogenesis. 29 (10): 1950–1954. doi:10.1093/carcin/bgn160. PMC 2556967. PMID 18641401.
- Kawai Y, Moriyama A, Asai K, Coleman-Campbell CM, Sumi S, Morishita H, et al. (Apr 2005). "Molecular characterization of histidinemia: identification of four missense mutations in the histidase gene". Human Genetics. 116 (5): 340–346. doi:10.1007/s00439-004-1232-5. PMID 15806399. S2CID 33960184.
- Taylor RG, Garcia-Heras J, Sadler SJ, Lafreniere RG, Willard HF, Ledbetter DH, et al. (1991). "Localization of histidase to human chromosome region 12q22→q24.1 and mouse chromosome region 10C2→D1". Cytogenetics and Cell Genetics. 56 (3–4): 178–181. doi:10.1159/000133082. PMID 2055114.
- Aleman G, Ortiz V, Langley E, Tovar AR, Torres N (Jul 2005). "Regulation by glucagon of the rat histidase gene promoter in cultured rat hepatocytes and human hepatoblastoma cells". American Journal of Physiology. Endocrinology and Metabolism. 289 (1): E172 – E179. doi:10.1152/ajpendo.00584.2004. PMID 15741241.
External links
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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