|Calculated MW||28.2 kDa (267 aa, 1-244 aa + His Tag)|
|Other Names||Quinoid dihydropteridine reductase, DHPR, FLJ42391, PKU2, SDR33C1|
|Results||Specific activity: > 27 units/ml|
|Sequence||MGSSHHHHHH SSGLVPRGSH MGSMAAAAAA GEARRVLVYG GRGALGSRCV QAFRARNWWV ASVDVVENEE ASASIIVKMT DSFTEQADQV TAEVGKLLGE EKVDAILCVA GGWAGGNAKS KSLFKNCDLM WKQSIWTSTI SSHLATKHLK EGGLLTLAGA KAALDGTPGM IGYGMAKGAV HQLCQSLAGK NSGMPPGAAA IAVLPVTLDT PMNRKSMPEA DFSSWTPLEF LVETFHDWIT GKNRPSSGSL IQVVTTEGRT ELTPAYF|
|Storage||-20°C; 1 mg/ml solution in 20 mM Tris-HCl buffer (pH 8.0) containing 10% glycerol and 2 mM DTT|
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Provided below are standard protocols that you may find useful for product applications.
QDPR is a member of the short-chain dehydrogenases/reductase (SDR) family of enzymes. Functioning as a homodimer, QDPR plays an important role in the recycling of tetrahydrobiopterin (BH4), an essential cofactor for the hydroxylation of the aromatic amino acids (tryptophan, tyrosine and phenylalanine). More specifically, QDPR catalyzes the regeneration of BH4 from quinonoid dihydrobiopterin (qBH2), the product generated from the hydroxylation reactions. Mutations in the gene encoding QDPR can lead to phenylketonuria II. Recombinant human QDPR protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.
Dahl H.-H.M.,et al.Nucleic Acids Res. 15:1921-1932(1987).
Dahl H.-H.M.,et al.Submitted (JUL-1987) to the EMBL/GenBank/DDBJ databases.
Lockyer J.,et al.Proc. Natl. Acad. Sci. U.S.A. 84:3329-3333(1987).
Dianzani I.,et al.Hum. Mutat. 12:267-273(1998).
Hsiao K.-J.,et al.Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
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