Thermostability, hyperthermophilic enzyme stabilizers

Thermostable chaperonins are potentially useful for industrial application. In this article, methods to study archaeal chaperonins are discussed, which use as model systems recombinant forms of CpkA and CpkB from the hyperthermophilic archaeon Thermococcus kodakaraensis KODl, previously reported as Pyrococcus kodakaraensis KOD1. The enhancing effect of chaperonin on enzyme stability... 

Ramon-Maiques, S. Marina, A. Uriarte, M. Fita, L Rubio, V. The 1.5 A resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic Archaeon pyrococcus furio-sus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases. J. Mol. Biol., 299, 463-476 (2000)... 

Temperature and pressure extremes require different strategies. Cellular lipids, proteins and nucleic acids are sensitive to high temperatures. Hyperthermophile bacteria have ether lipids instead of the more hydrolysis sensitive ester lipids in mesophiles [13]. Enzymes from hyperthermophiles show an unusual thermostability in the laboratory, and an important aspect of protein chemistry research is to find out the stabilizing principles. Crude cell extracts of hyperthermophiles show the presence of heat inducible proteins, called chaperones, which assist in the folding of proteins during cellular synthesis. Molecular details for cold adaptation of enzymes have been reported but are less extensively studied [14]. 

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