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Histidine ammonia-lyase

Template:Infobox3cols/rowTemplate:Infobox3cols/rowTemplate:Infobox3cols/rowTemplate:Infobox3cols/row
Identifiers
SymbolsHAL ; HIS; HSTD
External IDsOMIM609457 MGI96010 HomoloGene68229 ChEMBL: 4003 GeneCards: HAL Gene
EC number4.3.1.3
Orthologs
SpeciesHumanMouse
Entrez303415109
EnsemblENSG00000084110ENSMUSG00000020017
UniProtP42357P35492
RefSeq (mRNA)NM_001258333NM_010401
RefSeq (protein)NP_001245262NP_034531
Location (UCSC)Chr 12:
96.37 – 96.39 Mb
Chr 10:
93.49 – 93.52 Mb
PubMed search[1][2]
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

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

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References

  1. ^ a b "Entrez Gene: histidine ammonia-lyase". 
  2. ^ 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. PMID 8530107. doi:10.1006/geno.1995.1219. 
  3. ^ 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. PMID 10220322. doi:10.1021/bi982929q. 

External links

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


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