Formyltetrahydrofolate synthetase. Substrate binding to monomeric subunits.
Formyltetrahydrofolate synthetase. Substrate binding to monomeric subunits.
复制标题
甲酰四氢叶酸合成酶。
DOI：
10.1021/bi00753a006
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发表时间：
1972
期刊：
影响因子：
2.9
通讯作者：
J. Rabinowitz
中科院分区：
文献类型：
--
作者：
N. Curthoys;L. D'Ari Straus;J. Rabinowitz
Norman P. Curthoys, f Linda D’Ari Straus, and Jesse C. Rabinowitzt abstract: Formyltetrahydrofolate synthetase isolated from Clostridium cylindrosporum has a tetrameric structure and con-tains four nucleotide and four folate binding sites. The enzyme can be dissociated into catalytically inactive monomers by dialysis to remove monovalent cations. Substrate binding experiments were performed with the monomeric enzyme. Monomers that can be reassociatedand reactivated bind nucleotides with an affinity equivalent to native tetramer. Therefore, the nucleotide site is notaltered by dissociation or formyltetrahydrofolate synthetase isolated from Clostrid-ium cylindrosporum has a tetrameric structure and a molecular weight of 240,000 (Scott and Rabinowitz, 1967). MacKenzie and Rabinowitz (1971) have obtained evidence that the four
