Halophilic malate dehydrogenase--a case history of biophysical investigations: ultracentrifugation, light-, X-ray- and neutron scattering
- PMID: 1445401
Halophilic malate dehydrogenase--a case history of biophysical investigations: ultracentrifugation, light-, X-ray- and neutron scattering
Abstract
Halophilic malate dehydrogenase (hMDH) from Haloarcula marismortui has been isolated, purified and characterized by biochemical and biophysical solution studies. A stabilization mechanism at extremely high concentrations of salt, based on the formation of co-operative hydrate bonds between the protein and hydrated salt ions, was suggested from thermodynamic analysis of native enzyme solutions. Recently the gene coding for hMDH was isolated and sequenced and an active enzyme cloned (F. Cendrin, J. Chroboczek, G. Zaccai, H. Eisenberg and M. Mevarech, unpublished work). A study of the crystal structure of hMDH in a high-salt physiological medium is in progress (O. Butbul-Dym & J. Sussman, personal communication). Here we discuss in depth implications of these recent developments on our earlier results.
Similar articles
-
Solution structure of halophilic malate dehydrogenase from small-angle neutron and X-ray scattering and ultracentrifugation.J Mol Biol. 1986 Jul 5;190(1):97-106. doi: 10.1016/0022-2836(86)90078-1. J Mol Biol. 1986. PMID: 3783699
-
Stabilization of halophilic malate dehydrogenase.J Mol Biol. 1989 Aug 5;208(3):491-500. doi: 10.1016/0022-2836(89)90512-3. J Mol Biol. 1989. PMID: 2795658
-
Structure and activity of malate dehydrogenase from the extreme halophilic bacteria of the Dead Sea. 2. Inactivation, dissociation and unfolding at NaCl concentrations below 2 M. Salt, salt concentration and temperature dependence of enzyme stability.Eur J Biochem. 1981 Sep 1;118(3):471-7. doi: 10.1111/j.1432-1033.1981.tb05543.x. Eur J Biochem. 1981. PMID: 7297557
-
Life in unusual environments: progress in understanding the structure and function of enzymes from extreme halophilic bacteria.Arch Biochem Biophys. 1995 Apr 1;318(1):1-5. doi: 10.1006/abbi.1995.1196. Arch Biochem Biophys. 1995. PMID: 7726549 Review.
-
Halophilic enzymes: proteins with a grain of salt.Biophys Chem. 2000 Aug 30;86(2-3):155-64. doi: 10.1016/s0301-4622(00)00126-5. Biophys Chem. 2000. PMID: 11026680 Review.
Cited by
-
Density contrast sedimentation velocity for the determination of protein partial-specific volumes.PLoS One. 2011;6(10):e26221. doi: 10.1371/journal.pone.0026221. Epub 2011 Oct 20. PLoS One. 2011. PMID: 22028836 Free PMC article.
-
On the distribution of protein refractive index increments.Biophys J. 2011 May 4;100(9):2309-17. doi: 10.1016/j.bpj.2011.03.004. Biophys J. 2011. PMID: 21539801 Free PMC article.
-
The molecular refractive function of lens γ-Crystallins.J Mol Biol. 2011 Aug 19;411(3):680-99. doi: 10.1016/j.jmb.2011.06.007. Epub 2011 Jun 12. J Mol Biol. 2011. PMID: 21684289 Free PMC article.