title: Characterization of ATPase activity of class II chaperonin from the hyperthermophilic archaeon Pyrococcus furiosus.
abstract: To understand how molecular damage under harsh environmental conditions can be controlled, we investigated the properties of ATPase activity of the chaperonin molecular machinery from the hyperthermophilic archaeon Pyrococcus furiosus (PfCPN). PfCPN ATPase activity depended on K(+) and Mg(2+) and its optimal pH was 7.5. PfCPN had almost no ADPase activity. ADP strongly competitively inhibited PfCPN ATPase activity. Inhibition of PfCPN ATPase decreased its chaperonin activity in protecting lysozyme from heat-induced inactivation.
authors: Institute for Biological Sciences, Jiangsu University, Zhenjiang, Jiangsu, 212013, China. hyc@ujs.edu.cn
authors: Hua-you
authors: HY
authors: Chen
authors: Xiao-li
authors: XL
authors: Tan
authors: Jian
authors: J
authors: Lu
authors: Chun-xia
authors: CX
authors: Zhang
authors: Yi
authors: Y
authors: Zhang
authors: Sheng-li
authors: SL
authors: Yang
mesh_terms: D000244:Adenosine Diphosphate / Q000494:pharmacology; D000249:Adenosine Monophosphate / Q000494:pharmacology; D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D019843:Archaeal Proteins / Q000378:metabolism*; D002413:Cations, Divalent / Q000494:pharmacology; D002414:Cations, Monovalent / Q000494:pharmacology; D018833:Chaperonins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration / Q000187:drug effects; D008274:Magnesium / Q000494:pharmacology; D011188:Potassium / Q000494:pharmacology; D020027:Pyrococcus furiosus / Q000187:drug effects / Q000201:enzymology*; D013379:Substrate Specificity / Q000187:drug effects; D013696:Temperature
chemical_list: D019843:Archaeal Proteins; D002413:Cations, Divalent; D002414:Cations, Monovalent; D000249:Adenosine Monophosphate; D000244:Adenosine Diphosphate; D000251:Adenosine Triphosphatases; D018833:Chaperonins; D008274:Magnesium; D011188:Potassium