Histidine ammonia-lyase

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HAL
Identifiers
Aliases HAL, HIS, HSTD, histidine ammonia-lyase, Histidine ammonia-lyase
External IDs OMIM: 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
Band 12q23.1 Start 95,972,662 bp[1]
End 95,996,365 bp[1]
Orthologs
Species Human Mouse
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 Mb Chr 12: 93.49 – 93.52 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse
histidine ammonia-lyase
1gkm.jpg
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

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[edit]

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 an electrophilic co-factor which is formed autocatalytically by cyclization of the protein backbone of the enzyme.[7]

Pathology[edit]

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

References[edit]

  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[edit]

External links[edit]

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