Thermostability and thermoactivity of enzymes from hyperthermophilic Archaea

Bioorg Med Chem. 1994 Jul;2(7):659-67. doi: 10.1016/0968-0896(94)85015-1.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Archaea / classification*
  • Archaea / enzymology*
  • Archaea / genetics
  • DNA-Directed DNA Polymerase / chemistry
  • DNA-Directed DNA Polymerase / isolation & purification
  • DNA-Directed DNA Polymerase / metabolism*
  • Enzyme Stability
  • Hot Temperature
  • Hydrolases / chemistry
  • Hydrolases / isolation & purification
  • Hydrolases / metabolism*
  • Kinetics
  • Oxidoreductases / chemistry
  • Oxidoreductases / isolation & purification
  • Oxidoreductases / metabolism*
  • Phylogeny
  • Thermodynamics

Substances

  • Oxidoreductases
  • DNA-Directed DNA Polymerase
  • Hydrolases