DPYS
DPYS (dihydropyrimidinase, also known as DHPase) is a metallo-dependent hydrolase that catalyses the second step of reductive pyrimidine degradation. It opens the ring of dihydropyrimidines and is encoded by the DPYS gene, which is linked to dihydropyrimidinuria. Browse Assay Genie's current range of DPYS research reagents below, or read on for the biology behind the target.
DPYS catalyses the second step of the reductive pyrimidine degradation pathway: the reversible hydrolytic ring opening of dihydropyrimidines. It can open the ring of 5,6-dihydrouracil to give N-carbamyl-alanine, and the ring of 5,6-dihydrothymine to give N-carbamyl-amino isobutyrate. NCBI Gene describes the reaction as the conversion of 5,6-dihydrouracil to 3-ureidopropionate in pyrimidine metabolism. The enzyme therefore sits within the route by which cells break down uracil and thymine.
The protein belongs to the metallo-dependent hydrolases superfamily and the hydantoinase/dihydropyrimidinase family. HGNC places it in the M38 metallopeptidases gene group. Human DPYS is a 519-amino-acid protein. RefSeq reports that dihydropyrimidinase is expressed at a high level in liver and kidney, as a major 2.5-kb transcript and a minor 3.8-kb transcript. Mouse and rat each carry an orthologous gene, Dpys, so rodent models can be used to study the enzyme.
Defects in the DPYS gene are linked to dihydropyrimidinuria, which makes the gene and its product relevant to inherited disorders of pyrimidine metabolism. Researchers working on this area often study DPYS together with other enzymes of the same degradation pathway. They may also look at the related dihydropyrimidinase-like proteins DPYSL2, DPYSL3 and DPYSL4. Whether you are looking for a DPYS antibody, a DPYS ELISA kit or recombinant DPYS protein, the gene and enzyme information above is a useful starting point for experimental design.
DPYS catalyses the second step of reductive pyrimidine degradation, making it a key enzyme for studying how uracil and thymine are broken down.
Defects in the DPYS gene are linked to dihydropyrimidinuria, so the enzyme is relevant to work on this inherited metabolic condition.
Dihydropyrimidinase is expressed at a high level in liver and kidney, which makes these tissues a focus for expression studies.
As a member of the hydantoinase/dihydropyrimidinase family, DPYS is used to examine reversible hydrolytic ring opening of dihydropyrimidine substrates.
DPYS catalyses the second step of reductive pyrimidine degradation, the reversible hydrolytic ring opening of dihydropyrimidines. It can convert 5,6-dihydrouracil to N-carbamyl-alanine and 5,6-dihydrothymine to N-carbamyl-amino isobutyrate. NCBI Gene describes the product from dihydrouracil as 3-ureidopropionate.
DPYS is the HGNC-approved symbol for dihydropyrimidinase, and DHPase is a commonly used alias. The enzyme carries the EC number 3.5.2.2. It should not be confused with the dihydropyrimidinase-like proteins DPYSL2, DPYSL3 and DPYSL4, which are encoded by separate genes.
Mouse and rat both have an orthologous Dpys gene. In humans, defects in the DPYS gene are linked to dihydropyrimidinuria. Check the datasheet of any product for its validated reactivity before using it with a particular species.
Dihydropyrimidinase-like proteins related to DPYS, with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q14117; product specifications from Assay Genie datasheets.