Fraction of enolase activity recovered upon dilution from denaturant within 1 min

Range in the absence of chaperones ~55%: with chaperone ~100% % of enzyme activity
Organism Bacteria Escherichia coli
Reference Kerner MJ, Naylor DJ, Ishihama Y, Maier T, Chang HC, Stines AP, Georgopoulos C, Frishman D, Hayer-Hartl M, Mann M, Hartl FU. Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli. Cell. 2005 Jul 29 122(2):209-20. p.210 right column top paragraphPubMed ID16051146
Comments "As shown representatively for ENO, upon dilution from denaturant under standard conditions (37°C, 0.5µM final concentration), ~55% of enzyme activity was recovered within 1 min in the absence of chaperones (Figure 1A). Nearly 100% of enzyme activity was regained when either the DnaK system (DnaK, DnaJ, GrpE) or GroEL/GroES or GroEL alone was added with Mg-ATP (Figure 1A)."
Entered by Uri M
ID 110577