Abstract:
:Sepiapterin reductase (7,8-dihydrobiopterin: NADP+ oxidoreductase, EC 1.1.1.153) catalyzes the terminal step in the biosynthetic pathway for tetrahydrobiopterin, the cofactor necessary for aromatic amino acid hydroxylation. We report here the isolation of a cDNA clone for rat liver sepiapterin reductase. The cDNA has been excised from a lambda vector and the DNA sequence was determined. The insert contains the coding sequence for at least 95% of the rat enzyme and is fused to the Escherichia coli beta-galactosidase N-terminal segment and the lac promoter. The N-terminal region of the clone contains an extraordinarily high G + C content. The amino acid sequence deduced from the clone is in agreement with the size and composition of the enzyme and was matched to several tryptic peptide sequences. The enzyme encoded by the cDNA insert was shown to have sepiapterin reductase activity after expression in E. coli. Structural similarities were identified between this protein and several enzymes that should contain similar nucleotide and pteridine binding sites.
journal_name
Proc Natl Acad Sci U S Aauthors
Citron BA,Milstien S,Gutierrez JC,Levine RA,Yanak BL,Kaufman Sdoi
10.1073/pnas.87.16.6436subject
Has Abstractpub_date
1990-08-01 00:00:00pages
6436-40issue
16eissn
0027-8424issn
1091-6490journal_volume
87pub_type
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更新日期:1975-06-01 00:00:00