Hydantoinase/dihydropyrimidinase
IPR011778
Definition
Dihydropyrimidinase (DHPase) catalyses the second step of the reductive pyrimidine degradation, the reversible hydrolytic ring opening of dihydropyrimidines PMID:12626710. 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 PMID:7765480. 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 PMID:11092864. 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 related activity accounts for its participation in neuronal growth cone signaling PMID:9375656. CRMP3 has histone H4 deacetylase activity PMID:23443259.
6 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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