Primary structure of a folate-dependent trifunctional enzyme from Spodoptera frugiperda.
The dehydrogenase and synthetase activities of the NADP-dependent methylenetetra-hydrofolate dehydrogenase-cyclohydrolase-synthetase are undetectable in extracts of the Spodoptera frugiperda cell line, Sf9. However, a single cDNA encoding this protein was isolated from a library and sequenced. The deduced amino acid sequence codes for a protein of 933 amino acids in length that shows 59% identity to the human enzyme. The cDNA inserted in the yeast expression vector pVT102-U complements a purine auxotrophic yeast strain lacking this enzyme.
Tremblay
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GB
Department of Biochemistry, McGill University, Montreal, Quebec, Canada.
MacKenzie
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RE
D000595:Amino Acid Sequence; D000619:Aminohydrolases / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D016384:Consensus Sequence; D018076:DNA, Complementary / Q000235:genetics*; D005574:Formate-Tetrahydrofolate Ligase / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D017344:Genes, Insect; D008754:Methylenetetrahydrofolate Dehydrogenase (NADP) / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis; D012441:Saccharomyces cerevisiae; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D018411:Spodoptera / Q000201:enzymology* / Q000235:genetics
D018076:DNA, Complementary; D009097:Multienzyme Complexes; D011993:Recombinant Fusion Proteins; C021836:formyl-methenyl-methylenetetrahydrofolate synthetase; D008754:Methylenetetrahydrofolate Dehydrogenase (NADP); D000619:Aminohydrolases; D005574:Formate-Tetrahydrofolate Ligase