Biology:Histidine ammonia-lyase
 Generic protein structure example |
| histidine ammonia-lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Histidine ammonia-lyase homotetramer, Pseudomonas putida | |||||||||
| Identifiers | |||||||||
| EC number | 4.3.1.3 | ||||||||
| CAS number | 9013-75-6 | ||||||||
| 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 | ||||||||
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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.[1][2] 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.[1] 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.[3]
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
- ↑ 1.0 1.1 "Entrez Gene: histidine ammonia-lyase". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3034.
- ↑ "Molecular cloning and structural characterization of the human histidase gene (HAL)". Genomics 29 (1): 98–104. September 1995. 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 reading
- "Molecular cloning of a cDNA encoding human histidase". Biochim. Biophys. Acta 1216 (2): 293–5. 1993. doi:10.1016/0167-4781(93)90157-9. PMID 7916645.
- "New genetic associations detected in a host response study to hepatitis B vaccine". Genes Immun. 11 (3): 232–8. 2010. doi:10.1038/gene.2010.1. PMID 20237496.
- "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. 2004. doi:10.1101/gr.2596504. PMID 15489334.
- "Histidase expression in human epidermal keratinocytes: regulation by differentiation status and all-trans retinoic acid". J. Dermatol. Sci. 50 (3): 209–15. 2008. doi:10.1016/j.jdermsci.2007.12.009. PMID 18280705.
- "A role for ultraviolet radiation immunosuppression in non-melanoma skin cancer as evidenced by gene-environment interactions". Carcinogenesis 29 (10): 1950–4. 2008. doi:10.1093/carcin/bgn160. PMID 18641401.
- "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. 2002. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- "Molecular characterization of histidinemia: identification of four missense mutations in the histidase gene". Hum. Genet. 116 (5): 340–6. 2005. doi:10.1007/s00439-004-1232-5. PMID 15806399.
- "Localization of histidase to human chromosome region 12q22→q24.1 and mouse chromosome region 10C2→D1". Cytogenet. Cell Genet. 56 (3–4): 178–81. 1991. doi:10.1159/000133082. PMID 2055114.
- "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. 2005. doi:10.1152/ajpendo.00584.2004. PMID 15741241.
External links
- Histidine+Ammonia-Lyase 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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