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Histidine ammonia-lyase

HAL
Identifiers
AliasesHAL, HIS, HSTD, histidine ammonia-lyase, Histidine ammonia-lyase
External IDsOMIM: 609457 MGI: 96010 HomoloGene: 68229 GeneCards: HAL
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for HAL
Genomic location for HAL
Band12q23.1Start95,972,662 bp[1]
End95,996,365 bp[1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
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 MbChr 10: 93.49 – 93.52 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse
histidine ammonia-lyase
1gkm.jpg
Histidine ammonia-lyase homotetramer, Pseudomonas putida
Identifiers
EC number4.3.1.3
CAS number9013-75-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

Histidine ammonia-lyase (or histidase, or histidinase) is an enzyme that in humans is encoded by the HAL gene.[5][6] 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.[5] The reaction is catalyzed by 3,5-dihydro-5-methyldiene-4H-imidazol-4-one, an electrophilic co-factor 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.

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000084110 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020017 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:".
  4. ^ "Mouse PubMed Reference:".
  5. ^ a b "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, 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

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.