Histidine ammonia-lyase

HAL
Identifiers
Aliases	HAL, HIS, HSTD, histidine ammonia-lyase, Histidine ammonia-lyase
External IDs	OMIM: 609457 MGI: 96010 HomoloGene: 68229 GeneCards: HAL
Gene ontology Molecular function • catalytic activity • lyase activity • ammonia-lyase activity • histidine ammonia-lyase activity Cellular component • cytosol • cytoplasm Biological process • histidine metabolic process • histidine catabolic process to glutamate and formate • histidine catabolic process to glutamate and formamide • histidine catabolic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	3034	15109
Ensembl	ENSG00000084110	ENSMUSG00000020017
UniProt	P42357	P35492
RefSeq (mRNA)	NM_001258333 NM_001258334 NM_002108	NM_010401
RefSeq (protein)	NP_001245262.1 NP_001245263.1 NP_002099.1	NP_034531.1
Location (UCSC)	Chr 12: 95.97 – 96 Mb	Chr 10: 93.49 – 93.52 Mb
PubMed search
Wikidata
View/Edit Human		View/Edit Mouse

histidine ammonia-lyase
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 / EGO
Search PMC articles PubMed articles NCBI proteins

Histidine ammonia-lyase (or histidase, or histidinase) is an enzyme that in humans is encoded by the HAL gene. Histidase converts histidine into ammonia and urocanic acid.

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. The reaction is catalyzed by an electrophilic co-factor which is formed autocatalytically by cyclization of the protein backbone of the enzyme.

Pathology

Mutations in the gene for histidase are associated with histidinemia and urocanic aciduria.

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. 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. 
• 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. 
• 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 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.