Bivalent cations and amino-acid composition contribute to the thermostability ofBacillus licheniformisxylose isomerase
Open Access
- 1 December 2001
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 268 (23) , 6291-6301
- https://doi.org/10.1046/j.0014-2956.2001.02587.x
Abstract
Comparative analysis of genome sequence data from mesophilic and hyperthermophilic micro‐organisms has revealed a strong bias against specific thermolabile amino‐acid residues (i.e. N and Q) in hyper...Keywords
This publication has 40 references indexed in Scilit:
- Hyperthermophilic Enzymes: Sources, Uses, and Molecular Mechanisms for ThermostabilityMicrobiology and Molecular Biology Reviews, 2001
- Thermostabilization of a chimeric enzyme by residue substitutions: four amino acid residues in loop regions are responsible for the thermostability of Thermus thermophilus isopropylmalate dehydrogenaseBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2001
- [34] Structural basis of thermostability in hyperthermophilic proteins, or “There's more than one way to skin a cat”Published by Elsevier ,2001
- Selected Mutations in a Mesophilic Cytochrome cConfer the Stability of a Thermophilic CounterpartPublished by Elsevier ,2000
- Structural and Genomic Correlates of HyperthermostabilityJournal of Biological Chemistry, 2000
- Structural distribution of stability in a thermophilic enzymeProceedings of the National Academy of Sciences, 1999
- Influence of polymolecular events on inactivation behavior of xylose isomerase fromThermotoga neapolitana 5068Biotechnology & Bioengineering, 1999
- Comparing the Thermodynamic Stabilities of a Related Thermophilic and Mesophilic EnzymeBiochemistry, 1999
- Finding and using hyperthermophilic enzymesTrends in Biotechnology, 1998
- The stability of salt bridges at high temperatures: implications for hyperthermophilic proteins 1 1Edited by B. HonigJournal of Molecular Biology, 1998