Folate in demethylation: The crystal structure of the rat dimethylglycine dehydrogenase complexed with tetrahydrofolate
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- 作者：Zigmund Lukaa ; z.luka@vanderbilt.edu" class="auth_mail ; Svetlana Pakhomovab ; Lioudmila V. Loukachevitcha ; Marcia E. Newcomerb ; Conrad Wagnera
- 关键词：DMGDH ; dimethylglycine dehydrogenase ; DMG ; dimethylglycine ; THF ; tetrahydrofolate
- 刊名：Biochemical and Biophysical Research Communications
- 出版年：11 July 2014
- 年：2014
- 卷：449
- 期：4
- 页码：392-398
- 全文大小：1625 K
文摘
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DMGDH is an important enzyme in one-carbon metabolism.
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Bound tetrahydrofolate (THF) serves as a scavenger for the formaldehyde product.
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We solved the crystal structure of DMGDH and DMGDH–THF complex.
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An intramolecular channel connects the active site and the THF binding site.
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A mechanism for human DMGDH inactivation by a natural mutation is proposed.