Roitel O, Bec N, Lange R, Balny C, Branlant G
Maturation des ARN et Enzymologie Moléculaire, UMR 7567 CNRS-Université Henri Poincaré, Nancy I, Boulevard des Aiguillettes, Vandoeuvre-lès-Nancy, 54506, France.
Biochem Biophys Res Commun. 2001 May 4;283(2):347-50. doi: 10.1006/bbrc.2001.4779.
The effects of hydrostatic pressure on apo wild-type glyceraldehyde-3-phosphate dehydrogenase (wtGAPDH) from Bacillus stearothermophilus (B. stearothermophilus) have been studied by fluorescence spectroscopy under pressure from 0.1 to 650 MPa. Unlike yeast GAPDH [Ruan, K. C., and Weber, G. (1989) Biochemistry 28, 2144-2153], denaturation of the tetrameric apo wtGAPDH from B. stearothermophilus is likely to precede dissociation into subunits. As expected, denaturation is accompanied by the loss of enzymatic activity. B. stearothermophilus apo wtGAPDH interfaces are less pressure sensitive than apo yeast GAPDH ones, while NAD does not protect B. stearothermophilus wtGAPDH against denaturation by pressure. The pressure effects on B. stearothermophilus GAPDH whose R and Q-axis interfaces were destabilized by disruption of interfacial hydrogen bonds are similar to that of apo wtGAPDH.
通过荧光光谱法，在0.1至650MPa的压力下研究了静水压力对嗜热脂肪芽孢杆菌（B. stearothermophilus）的载脂蛋白野生型甘油醛-3-磷酸脱氢酶（wtGAPDH）的影响。与酵母GAPDH[Ruan, K. C., and Weber, G. (1989) Biochemistry 28, 2144 - 2153]不同，嗜热脂肪芽孢杆菌的四聚体载脂蛋白wtGAPDH的变性可能先于其解离成亚基。正如预期的那样，变性伴随着酶活性的丧失。嗜热脂肪芽孢杆菌载脂蛋白wtGAPDH的界面比载脂蛋白酵母GAPDH的界面压力敏感性更低，而NAD不能保护嗜热脂肪芽孢杆菌wtGAPDH免受压力导致的变性。对嗜热脂肪芽孢杆菌GAPDH的压力影响，其R轴和Q轴界面因界面氢键的破坏而不稳定，这与载脂蛋白野生型GAPDH的情况相似。
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