v5.1.0.3
Glycine data from LIS
Type | Family |
Description | Dihydropyrimidinase (DHPase) catalyses the second step of the reductive pyrimidine degradation, the reversible hydrolytic ring opening of dihydropyrimidines [ ]. Primarily converts 5,6-dihydrouracil to N-carbamyl-beta-alanine (also called 3-ureidopropanoate) but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme [].This entry represents the hydantoinase/dihydropyrimidinase family, which also includes D-phenylhydantoinases. This enzyme catalyses the stereospecific hydrolysis of the cyclic amide bond of D-hydantoin derivatives with an aromatic side chains at the 5'-position, and has no activity on dihydropyrimidines [ ].Dihydropyrimidinase-related proteins (collapsin response mediator proteins, CRMPs) share sequence similarity with liver DHPase. Although purified CRMP does not hydrolyse DHPase substrates, it is likely that a relatedactivity accounts for its participation in neuronal growth cone signaling [ ]. CRMP3 has histone H4 deacetylase activity []. |
Short Name | Hydantoinase/dihydroPyrase |