Britton K L, Stillman T J, Yip K S, Forterre P, Engel P C, Rice D W
The Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, United Kingdom.
J Biol Chem. 1998 Apr 10;273(15):9023-30. doi: 10.1074/jbc.273.15.9023.
A homology-based modeling study on the extremely halophilic glutamate dehydrogenase from Halobacterium salinarum has been used to provide insights into the molecular basis of salt tolerance. The modeling reveals two significant differences in the characteristics of the surface of the halophilic enzyme that may contribute to its stability in high salt. The first of these is that the surface is decorated with acidic residues, a feature previously seen in structures of halophilic enzymes. The second is that the surface displays a significant reduction in exposed hydrophobic character. The latter arises not from a loss of surface-exposed hydrophobic residues, as has previously been proposed, but from a reduction in surface-exposed lysine residues. This is the first report of such an observation.
一项针对盐生盐杆菌中极端嗜盐谷氨酸脱氢酶的基于同源性的建模研究，旨在深入了解耐盐性的分子基础。该建模揭示了嗜盐酶表面特征的两个显著差异，这可能有助于其在高盐环境中的稳定性。其中第一个差异是，其表面布满酸性残基，这是嗜盐酶结构中先前已观察到的一个特征。第二个差异是，其表面暴露的疏水特性显著降低。后者并非如先前所提出的那样源于表面暴露的疏水残基的丧失，而是源于表面暴露的赖氨酸残基的减少。这是关于此类观察结果的首次报道。
