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Large improvement in the thermal stability of a tetrameric malate dehydrogenase by single point mutations at the dimer-dimer interface.

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Protein Data Bank Japan2023-12-13 更新2026-03-21 收录
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https://pdbj.org/mine/summary/1uxg
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Large improvement in the thermal stability of a tetrameric malate dehydrogenase by single point mutations at the dimer-dimer interface. Descriptor: FUMARIC ACID, MALATE DEHYDROGENASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE Authors: Bjork, A, Dalhus, B, Mantzilas, D, Eijsink, V.G.H, Sirevag, R. Deposit date: 2004-02-25 Release date: 2004-08-26 Last modified: 2023-12-13 Method: X-RAY DIFFRACTION (1.9 Å) Cite: Large Improvement in the Thermal Stability of a Tetrameric Malate Dehydrogenase by Single Point Mutations at the Dimer-Dimer Interface. J.Mol.Biol., 341, 2004

通过在二聚体-二聚体界面引入单点突变,可显著提升四聚体苹果酸脱氢酶(tetrameric malate dehydrogenase)的热稳定性。 关键词:延胡索酸(fumaric acid)、苹果酸脱氢酶(malate dehydrogenase)、烟酰胺腺嘌呤二核苷酸(nicotinamide-adenine-dinucleotide) 作者:Bjork, A、Dalhus, B、Mantzilas, D、Eijsink, V.G.H、Sirevag, R 提交日期:2004-02-25 发布日期:2004-08-26 末次修改日期:2023-12-13 实验方法:X射线衍射,分辨率1.9 Å 引用:通过二聚体-二聚体界面单点突变大幅提升四聚体苹果酸脱氢酶热稳定性. 《J.Mol.Biol.》, 341, 2004
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2004-02-25
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