Structural highlights
Publication Abstract from PubMed
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.
Molecular structure of a 5,10-methylenetetrahydrofolate dehydrogenase from the silkworm Bombyx mori.,Haque MR, Higashiura A, Nakagawa A, Hirowatari A, Furuya S, Yamamoto K FEBS Open Bio. 2019 Feb 26;9(4):618-628. doi: 10.1002/2211-5463.12595., eCollection 2019 Apr. PMID:30984537[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Haque MR, Higashiura A, Nakagawa A, Hirowatari A, Furuya S, Yamamoto K. Molecular structure of a 5,10-methylenetetrahydrofolate dehydrogenase from the silkworm Bombyx mori. FEBS Open Bio. 2019 Feb 26;9(4):618-628. doi: 10.1002/2211-5463.12595., eCollection 2019 Apr. PMID:30984537 doi:http://dx.doi.org/10.1002/2211-5463.12595
