From hyperthermophiles to psychrophiles: the structural basis of temperature stability of the amino acid dehydrogenases.
The determination and comparison of the structures of a number of glutamate dehydrogenases that span the spectrum of thermal stability from mesophiles to hyperthermophiles have revealed that the formation of extended ion-pair networks is a major stabilizing feature in the adaptation of the organism to life at 100 degrees C. Analysis of the structures of other hyperthermophilic proteins has shown that ion-pair networks also play roles in their stabilization, including the phosphoglucose isomerase from Pyrococcus furiosus and the maltosyltransferase from Thermotoga maritima.
Baker
P J
PJ
Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, U.K. P.Baker@sheffield.ac.uk
D050788:Alanine Dehydrogenase; D000594:Amino Acid Oxidoreductases / Q000737:chemistry*; D000596:Amino Acids / Q000737:chemistry; D005964:Glucosyltransferases / Q000737:chemistry; D005969:Glutamate Dehydrogenase / Q000737:chemistry*; D007477:Ions; D009154:Mutation; D020027:Pyrococcus furiosus / Q000201:enzymology; D012492:Salts / Q000737:chemistry; D020592:Shewanella / Q000201:enzymology; D013045:Species Specificity; D013696:Temperature; D020124:Thermotoga maritima / Q000201:enzymology; D014733:Vibrio / Q000201:enzymology
D000596:Amino Acids; D007477:Ions; D012492:Salts; D000594:Amino Acid Oxidoreductases; D050788:Alanine Dehydrogenase; D005969:Glutamate Dehydrogenase; D005964:Glucosyltransferases; C436710:maltosyltransferase