Member database | Pfam |
Pfam type | domain |
Short name | Urocanase_C |
Author | Bateman A;0000-0002-6982-4660 |
Sequence Ontology | 0000417 |
Description Imported from IPR035401
This entry represents the C-terminal domain found in Urocanase.
Urocanase
[2] (also known as imidazolonepropionate hydrolase or urocanate hydratase) is the enzyme that catalyses the second step in the degradation of histidine, the hydration of urocanate into imidazolonepropionate:
urocanate + H2O = 4,5-dihydro-4-oxo-5-imidazolepropanoate
Urocanase is found in some bacteria (gene hutU)
[1], 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 Imported from IPR035401
1.Urocanase and N-formimino-L-glutamate formiminohydrolase of Bacillus subtilis, two enzymes of the histidine degradation pathway. Kaminskas E, Kimhi Y, Magasanik B. J. Biol. Chem. 245, 3536-44, (1970). PMID: 4990470
2.The urocanase story: a novel role of NAD+ as electrophile. Retey J. Arch. Biochem. Biophys. 314, 1-16, (1994). View articlePMID: 7944380