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; OMA:HAL - orthologs
Gene location (Human) Chr. Chromosome 12 (human) [1] Band 12q23.1 Start 95,972,662 bp [1] End 95,996,365 bp [1]
Gene location (Mouse) Chr. Chromosome 10 (mouse) [2] Band 10 C2|10 48.49 cM Start 93,324,630 bp [2] End 93,355,166 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right lobe of liver human penis skin of thigh vulva blood oocyte skin of arm monocyte secondary oocyte skin of abdomen Top expressed in morula skin of external ear left lobe of liver lip skin of back lumbar spinal ganglion calvaria umbilical cord spermatid granulocyte More reference expression data BioGPS n/a
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 NP_001245263 NP_002099 NP_034531 Location (UCSC) Chr 12: 95.97 – 96 Mb Chr 10: 93.32 – 93.36 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

histidine ammonia-lyase
Histidine ammonia-lyase homotetramer, Pseudomonas putida
Identifiers
EC no.	4.3.1.3
CAS no.	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
Search PMC articles PubMed articles NCBI proteins

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]

Proposed autocatalytic formation of MIO cofactor in another enzyme, phenylalanine ammonia-lyase, from the tripeptide Ala-Ser-Gly by two water elimination steps.

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. GRCh38: Ensembl release 89: ENSG00000084110 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000020017 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: histidine ammonia-lyase".
6. 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.
7. 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

• 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.