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Structure and expression of human dihydropteridine reductase.
Dihydropteridine reductase (DHPR; EC 1.6.99.7) catalyzes the NADH-mediated reduction of quinonoid dihydrobiopterin and is an essential component of the pterin-dependent aromatic amino acid hydroxylating systems. A cDNA for human DHPR was isolated from a human liver cDNA library in the vector lambda gt11 using a monospecific antibody against sheep DHPR. The nucleic acid sequence and amino acid sequence of human DHPR were determined from a full-length clone. A 112 amino acid sequence of sheep DHPR was obtained by sequencing purified sheep DHPR. This sequence is highly homologous to the predicted amino acid sequence of the human protein. Gene transfer of the recombinant human DHPR into COS cells leads to expression of DHPR enzymatic activity. These results indicate that the cDNA clone identified by antibody screening is an authentic and full-length cDNA for human DHPR.
PMID: 3033643 [PubMed - indexed for MEDLINE]
PMCID: PMC304863
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Cited by 8 PubMed Central articles
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Two new mutations in the dihydropteridine reductase gene in patients with tetrahydrobiopterin deficiency.
Dianzani I, Howells DW, Ponzone A, Saleeba JA, Smooker PM, Cotton RG.
J Med Genet. 1993 Jun; 30(6):465-9.
[J Med Genet. 1993]
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Hyperphenylalaninemia due to defects in tetrahydrobiopterin metabolism: molecular characterization of mutations in 6-pyruvoyl-tetrahydropterin synthase.
Thöny B, Leimbacher W, Blau N, Harvie A, Heizmann CW.
Am J Hum Genet. 1994 May; 54(5):782-92.
[Am J Hum Genet. 1994]
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High-level expression of human dihydropteridine reductase (EC 1.6.99.7), without N-terminal amino acid protection, in Escherichia coli.
Armarego WL, Cotton RG, Dahl HH, Dixon NE.
Biochem J. 1989 Jul 1; 261(1):265-8.
[Biochem J. 1989]
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