Molecular structure of a 5,10‐methylenetetrahydrofolate dehydrogenase from the silkworm Bombyx mori
Molecular structure of a 5,10‐methylenetetrahydrofolate dehydrogenase from the silkworm Bombyx mori
复制标题
家蚕 5,10-亚甲基四氢叶酸脱氢酶的分子结构
作者：
M. Haque;A. Higashiura;A. Nakagawa;A. Hirowatari;S. Furuya;Kohji Yamamoto
酶5，10-亚甲基四氢叶酸脱氢酶（MTHFD）对于某些氨基酸（甘氨酸、丝氨酸和甲硫氨酸）和核酸（胸苷酸和嘌呤）的产生至关重要。在这里，我们确定了一个cDNA编码这种酶从家蚕家蚕。重组B. B.在大肠杆菌中表达的mori MTHFD（bmMTHFD）在NADP+和NAD+存在下识别5，10-亚甲基四氢叶酸和5，10-亚甲基四氢叶酸作为底物。通过X射线晶体学以1.75 μ m的分辨率测定bmMTHFD结构。定点突变表明氨基酸残基Tyr 49有助于其催化活性。我们的研究结果提供了深入了解的机制MTHFD的活动从B。桑和潜在的其它昆虫，并且因此可以促进对MTHFD具有特异性的抑制剂作为杀虫剂的开发。
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.
大鼠 C1-四氢叶酸合酶。
DOI：
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发表时间：
1990
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Thigpen,AE;West,MG;Appling,DR
通讯作者：
Appling,DR
新型真核单功能 NAD() 依赖性 5,10-亚甲基四氢叶酸脱氢酶的分离和表征。
影响因子：
2.9
作者：
Barlowe,CK;Appling,DR
通讯作者：
Appling,DR