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- W2484986857 abstract "C1-tetrahydrofolate (H4folate) synthase is a trifunctional protein possessing the activities 10-formyl-H4folate synthetase, 5,10-methenyl-H4folate cyclohydrolase, and 5,10-methylene-H4folate dehydrogenase. The current model divides the eukaryotic protein into two functionally independent domains with dehydrogenase/cyclohydrolase activities sharing an overlapping site on the N-terminal domain and synthetase activity associated with the C-terminal domain. In prokaryotes, these activities are generally catalyzed by separate monofunctional enzymes. The genes or cDNAs encoding members of this family of enzymes have been isolated from mammalian, yeast, and bacterial sources and reveal considerable conservation of amino acid sequence. In an effort to elucidate structure/function relationships in these proteins, we have utilized several recombinant DNA methodologies to dissect active site and domain structure in this family of enzymes. Site-directed and random mutagenesis has been used to identify important amino acid residues in the overlapping dehydrogenase/cyclohydrolase active site. Deletion analysis and construction and expression of chimeric forms of the trifunctional enzyme in which the two domains derive from different species have provided insights into domain structure and function." @default.
- W2484986857 created "2016-08-23" @default.
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- W2484986857 date "1993-07-23" @default.
- W2484986857 modified "2023-10-13" @default.
- W2484986857 title "C1-Tetrahydrofolate Synthase" @default.
- W2484986857 doi "https://doi.org/10.1021/bk-1993-0516.ch017" @default.
- W2484986857 hasPublicationYear "1993" @default.
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