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

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

研究成果: Contribution to journalArticle査読

4 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)618-628
ページ数11
ジャーナルFEBS Open Bio
9
4
DOI
出版ステータス出版済み - 4 2019

All Science Journal Classification (ASJC) codes

  • 生化学、遺伝学、分子生物学(全般)

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