Histidine ammonia-lyase
| HAL | |||
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Gene ontology | |||
| Molecular function | |||
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| Biological process | |||
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| Location (UCSC) | Chr 12: 95.97 – 96 Mb | Chr 10: 93.32 – 93.36 Mb | |||||||
| PubMed search | [3] | [4] | |||||||
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| histidine ammonia-lyase | |||||||||
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ExPASy NiceZyme view | | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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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
- Phenylalanine ammonia-lyase, another enzyme that contains the MIO cofactor
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".
- PMID 8530107.
- PMID 10220322.
Further reading
- Suchi M, Harada N, Wada Y, Takagi Y (1993). "Molecular cloning of a cDNA encoding human histidase". Biochim. Biophys. Acta. 1216 (2): 293–5. 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. 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. 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. 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. 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. 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. 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. 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. PMID 15741241.
External links
- Histidine+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.
