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Your search keyword '"5,10‐methylenetetrahydrofolate dehydrogenase"' showing total 2 results
Start Over Descriptor "5,10‐methylenetetrahydrofolate dehydrogenase" Topic insect proteins
2 results on '"5,10‐methylenetetrahydrofolate dehydrogenase"'

1. Molecular structure of a 5,10-methylenetetrahydrofolate dehydrogenase from the silkworm Bombyx mori .

Author

Haque MR, Higashiura A, Nakagawa A, Hirowatari A, Furuya S, and Yamamoto K

Subjects
Amino Acid Sequence, Animals, Bombyx enzymology, Bombyx metabolism, DNA, Complementary chemistry, DNA, Complementary genetics, DNA, Complementary metabolism, Escherichia coli genetics, Insect Proteins chemistry, Insect Proteins metabolism, Methylenetetrahydrofolate Dehydrogenase (NADP) chemistry, Methylenetetrahydrofolate Dehydrogenase (NADP) metabolism, Molecular Structure, Mutagenesis, Site-Directed, Phylogeny, Recombinant Proteins chemistry, Recombinant Proteins genetics, Recombinant Proteins metabolism, Sequence Alignment, Bombyx genetics, Insect Proteins genetics, Methylenetetrahydrofolate Dehydrogenase (NADP) genetics
Abstract

The enzyme 5,10-methylenetetrahydrofolate dehydrogenase (MTHFD) is essential for the production of certain amino acids (glycine, serine, and methionine) and nucleic acids (thymidylate and purine). Here, we identified a cDNA encoding this enzyme from the silkworm Bombyx mori . The recombinant B. mori MTHFD (bmMTHFD) expressed in Escherichia coli recognized 5,10-methylenetetrahydrofolate and 5,10-methenyltetrahydrofolate as substrate in the presence of NADP + as well as NAD + . The bmMTHFD structure was determined at a resolution of 1.75 Å by X-ray crystallography. Site-directed mutagenesis indicated that the amino acid residue Tyr49 contributed to its catalytic activity. Our findings provide insight into the mechanism underlying the activity of MTHFD from B. mori and potentially other insects and may therefore facilitate the development of inhibitors specific to MTHFD as insecticides., Competing Interests: The authors declare no conflict of interest.

Published
2019
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2. Molecular structure of a 5,10‐methylenetetrahydrofolate dehydrogenase from the silkworm Bombyx mori

Author

Kohji Yamamoto, Aiko Hirowatari, Akifumi Higashiura, Shigeki Furuya, Atsushi Nakagawa, and Mohammad R. Haque

Subjects
0301 basic medicine, crystal structure, DNA, Complementary, Dehydrogenase, General Biochemistry, Genetics and Molecular Biology, Serine, serine, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Oxidoreductase, Bombyx mori, Escherichia coli, 5,10‐methylenetetrahydrofolate dehydrogenase, Animals, Amino Acid Sequence, Research Articles, Phylogeny, chemistry.chemical_classification, Methylenetetrahydrofolate Dehydrogenase (NADP), Methionine, biology, Molecular Structure, fungi, biology.organism_classification, Bombyx, Recombinant Proteins, Amino acid, 030104 developmental biology, chemistry, Biochemistry, 030220 oncology & carcinogenesis, Glycine, Mutagenesis, Site-Directed, Insect Proteins, NAD+ kinase, Sequence Alignment, NADP, Research Article
Abstract

The enzyme 5,10-methylenetetrahydrofolate dehydrogenase (MTHFD) is essential for the production of certain amino acids (glycine, serine, and methionine) and nucleic acids (thymidylate and purine). Here, we identified a cDNA encoding this enzyme from the silkworm Bombyx mori. The recombinant B. mori MTHFD (bmMTHFD) expressed in Escherichia coli recognized 5,10-methylenetetrahydrofolate and 5,10-methenyltetrahydrofolate as substrate in the presence of NADP + as well as NAD +. The bmMTHFD structure was determined at a resolution of 1.75 A by X-ray crystallography. Site-directed mutagenesis indicated that the amino acid residue Tyr49 contributed to its catalytic activity. Our findings provide insight into the mechanism underlying the activity of MTHFD from B. mori and potentially other insects and may therefore facilitate the development of inhibitors specific to MTHFD as insecticides.

Published
2019

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