Urocanase

Urocanase
Crystal structure of Urocanase from B. subtilis.
Identifiers
Symbol	Urocanase
Pfam	PF01175
InterPro	IPR000193
PROSITE	PDOC00947
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Urocanic acid

Imidazol-4-one-5-propionic acid

Urocanase^[1] (also known as imidazolonepropionate hydrolase or urocanate hydratase) is the enzyme that catalyzes the second step in the degradation of histidine, the hydration of urocanate into imidazolonepropionate.

urocanate + H₂O 4,5-dihydro-4-oxo-5-imidazolepropanoate

Inherited deficiency of urocanase leads to elevated levels of urocanic acid in the urine, a condition known as urocanic aciduria.

Urocanase is found in some bacteria (gene hutU), in the liver of many vertebrates and has also been found in the plant Trifolium repens (white clover). Urocanase is a protein of about 60 Kd, it binds tightly to NAD⁺ and uses it as an electrophil cofactor. A conserved cysteine has been found to be important for the catalytic mechanism and could be involved in the binding of the NAD⁺.

References

External links

• Urocanate Hydratase at the US National Library of Medicine Medical Subject Headings (MeSH)
• EC 4.2.1.49