Histidine ammonia-lyase explained

histidine ammonia-lyase
Ec Number:4.3.1.3
Cas Number:9013-75-6
Go Code:0004397
Width:270

Histidine ammonia-lyase (histidase, histidinase) is an enzyme that in humans is encoded by the HAL gene.[1] [2] 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.[1] 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.[3]

Pathology

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

See also

Further reading

Notes and References

  1. Web site: Entrez Gene: histidine ammonia-lyase .
  2. Suchi M, Sano H, Mizuno H, Wada Y . Molecular cloning and structural characterization of the human histidase gene (HAL) . Genomics . 29 . 1 . 98–104 . September 1995 . 8530107 . 10.1006/geno.1995.1219 .
  3. Schwede. TF. Rétey. J. Schulz. GE. Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile.. Biochemistry. Apr 27, 1999. 38. 17. 5355–5361. 10220322. 10.1021/bi982929q.