Thermostability and thermoactivity of enzymes from hyperthermophilic Archaea.
Enzymes from hyperthermophilic microorganisms are characteristically thermostable and thermoactive at extremely high temperatures. Information about the basis for the structure and function of these novel proteins is beginning to emerge. However, there are very few generalizations that can be drawn at this point that can be derived from the limited number of studies that have focused on biocatalysis and thermostability at extremely high temperatures.
Department of Biochemistry, University of Georgia, Athens 30602-7229.
M W
MW
Adams
R M
RM
Kelly
D001105:Archaea / Q000145:classification* / Q000201:enzymology* / Q000235:genetics; D004259:DNA-Directed DNA Polymerase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D004795:Enzyme Stability; D006358:Hot Temperature; D006867:Hydrolases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D010088:Oxidoreductases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D010802:Phylogeny; D013816:Thermodynamics
D010088:Oxidoreductases; D004259:DNA-Directed DNA Polymerase; D006867:Hydrolases