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Histidine ammonia-lyase (or histidase, or histidinase) is an enzyme that in humans is encoded by the HAL gene.^[1]^[2] 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.^[1] The reaction is catalyzed by an electrophilic co-factor 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.

§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.

§References

^ ^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, 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.

§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.

This lyase article is a stub. You can help Wikipedia by expanding it.

English Journal

Effect of histidine administration to female rats during pregnancy and lactation on enzymes activity of phosphoryltransfer network in cerebral cortex and hippocampus of the offspring.

Rojas DB, de Andrade RB, Gemelli T, Oliveira LS, Campos AG, Dutra-Filho CS, Wannmacher CM.SourceDepartamento de Bioquímica, Programa de Pós-Graduação em Ciências Biológicas: Bioquímica, Instituto de Ciências Básicas da Saúde, Universidade Federal do Rio Grande do Sul, Rua Ramiro Barcelos, 2600 anexo, 90035-003, Porto Alegre, RS, Brazil.
Metabolic brain disease.Metab Brain Dis.2012 May 27. [Epub ahead of print]
Histidinemia is an inborn error of metabolism of amino acids caused by deficiency of histidase activity in liver and skin with consequent accumulation of histidine in plasma and tissues. Histidinemia is an autosomal recessive trait usually considered harmless to patients and their offspring, but som
PMID 22638695

Neonatal blue light phototherapy and melanocytic nevi: a twin study.

Csoma Z, Tóth-Molnár E, Balogh K, Polyánka H, Orvos H, Ocsai H, Kemény L, Széll M, Oláh J.SourceDepartment of Dermatology and Allergology, University of Szeged, Szeged, Hungary. csomazs@mail.derma.szote.u-szeged.hu
Pediatrics.Pediatrics.2011 Oct;128(4):e856-64. Epub 2011 Sep 19.
BACKGROUND: Neonatal blue light phototherapy (NBLP) has been widely and successfully used for the treatment of neonatal jaundice to reduce the plasma concentration of bilirubin and, hence, to prevent kernicterus. Only a few and controversial data are available in the literature as to how NBLP influe
PMID 21930537

Japanese Journal

Identification of the transcriptional regulatory gene of histidase and urocanase in Pseudomonas aeruginosa -Regulation of histidase and urocanase expression-

NAKADA Yuji
Aino journal 8, 19-23, 2009
… When wild-type P.aeruginosa PAO1 cells were cultured in minimal medium P (MMP) containing 20mM histidine, synthesis of histidase and urocanase was detected in crude extract at 3186±118 (U/mg-proteins) and 243±3 (10-3 U/mg-proteins), respectively. … In contrast, PAO4399, the spontaneous mutant of PAO1, can synthesize histidase and urocanase sufficiently under the nutrient conditions of MMP containing histidine or glutamate. …
NAID 110008730879

Histidase expression in human epidermal keratinocytes : Regulation by differentiation status and all-trans retinoic acid

ECKHART Leopold,SCHMIDT Martina,MILDNER Michael,MLITZ Veronika,ABTIN Arby,BALLAUN Claudia,FISCHER Heinz,MRASS Paul,TSCHACHLER Erwin
Journal of dermatological science 50(3), 209-215, 2008-06-01
NAID 10024119134

カエル舌水受容器の化学修飾2.DEP, AIおよびHNBBの作用

松本歯学 22(2), 134-140, 1996-08-31
… Our previous work demonstrated that histidase and tryptophanase applied to the single fungi form papilla preparation dissected from the frog tongue inhibited irreversibly the response to the stimulating solution containing 5mM CaCl_2 and 100mM NaCl (Ca response) without inhibiting the response to 0.3M NaSCN and 0.5M NaCl (Na response) in some preparations, suggesting that histidine and tryprophane residues of receptor molecules are essential for the initiation of the transduction process of the Ca response. …
NAID 80009265064

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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
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PMC	articles
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NCBI	proteins

Histidine ammonia-lyase
Identifiers
Symbols	HAL ; HIS; HSTD
External IDs	OMIM: 609457 MGI: 96010 HomoloGene: 68229 ChEMBL: 4003 GeneCards: HAL Gene
EC number	4.3.1.3
Gene ontology
Molecular function	• histidine ammonia-lyase activity;
Cellular component	• cytosol;
Biological process	• histidine catabolic process; • biosynthetic process; • histidine catabolic process to glutamate and formamide; • histidine catabolic process to glutamate and formate; • cellular nitrogen compound metabolic process; • small molecule metabolic process;
	Sources: Amigo / QuickGO
Orthologs
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