Catalyzing "hot" reactions: enzymes from hyperthermophilic Archaea.
We reflect on some of our studies on the hyperthermophilic archaeon, Thermococcus kodakaraensis KOD1 and its enzymes. The strain can grow at temperatures up to the boiling point and also represents one of the simplest forms of life. As expected, all enzymes displayed remarkable thermostability, and we have determined some of the basic principles that govern this feature. To our delight, many of the enzymes exhibited unique biochemical properties and novel structures not found in mesophilic proteins. Here, we focus on a few enzymes that are useful in application, and whose three-dimensional structures are characteristic of thermostable enzymes.
Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan. imanaka@sbchem.kyoto-u.ac.jp
Tadayuki
T
Imanaka
Haruyuki
H
Atomi
D011088:DNA Ligases / Q000737:chemistry*; D004259:DNA-Directed DNA Polymerase / Q000737:chemistry*; D004795:Enzyme Stability; D005969:Glutamate Dehydrogenase / Q000737:chemistry*; D006358:Hot Temperature; D008958:Models, Molecular; D019853:O(6)-Methylguanine-DNA Methyltransferase / Q000737:chemistry*; D012273:Ribulose-Bisphosphate Carboxylase / Q000737:chemistry; D019712:Thermococcus / Q000201:enzymology* / Q000254:growth & development
D005969:Glutamate Dehydrogenase; D019853:O(6)-Methylguanine-DNA Methyltransferase; D004259:DNA-Directed DNA Polymerase; D012273:Ribulose-Bisphosphate Carboxylase; D011088:DNA Ligases