3.6.4.10 15-deoxyspergualin stimulates the ATPase activity of mammalian and yeast cytosolic Hsc70 from 20 to 40%, no effect on HSC70 BiP and DnaJ-stimulated Hsc70 ATPase activity 210516 3.6.4.10 activator of Hsp90 ATPase Aha1, 5fold activation of intrinsic ATPase activity 656125 3.6.4.10 aggregated alpha-casein - 758438 3.6.4.10 aggregated glucose-6-phosphate dehydrogenase - 758438 3.6.4.10 aggregated RepE - 758438 3.6.4.10 Aha1 potent activator of the ATPase subunit of the enzyme 756203 3.6.4.10 Aha1 protein - 700378 3.6.4.10 Aha1p potent stimulator of the enzyme ATPase activity 757741 3.6.4.10 alpha-casein - 733304 3.6.4.10 Apg2 at low concentration (0.0004 mM), Agp2 stimulates the ATPase activity of the enzyme 757440 3.6.4.10 apo c cytosolic precursor of cytochrome c 210500 3.6.4.10 Asn-Asp-Leu-Leu-Leu-Thr-Gly approx. 5fold activation of ATPase activity by NRLLLTG peptide 656011 3.6.4.10 Asn-Asp-Leu-Leu-Leu-Thr-Gly peptide NRLLLTG, 5fold and 2fold increase in ATPase activity at pH 7.0 and pH 9.0, respectively 654656 3.6.4.10 ATP ATP binding to nucleotide-binding domain 1 serves as a central regulatory switch for the chaperone, it triggers binding of polypeptides and stimulates ATP hydrolysis in the C-terminal nucleotide-binding domain 2 by more than 2 orders of magnitude 688361 3.6.4.10 ATP in 1:1 mixture with ATP-gammaS, greatly stimulates protein remodeling 689141 3.6.4.10 ATP-gammaS in 1:1 mixture with ATP, greatly stimulates protein remodeling 689141 3.6.4.10 Bacillus subtilis ClpC adaptor protein MecA the refolding activity of SyClpC is enhanced 3fold in presence of Bacillus subtilis ClpC adaptor protein MecA 669512 3.6.4.10 casein - 733263 3.6.4.10 DnaJ - 210513, 210516 3.6.4.10 DnaJ interaction with DnaJ stimulates the hydrolysis of ATP by DnaK 210513 3.6.4.10 EhAha1c co-chaperone Aha1, i.e. activator of Hsp90 ATPase, lacking a canonical Aha1 N-terminal domain compared to other Aha1 co-chaperones. EhAha1c is capable of binding and stimulating ATPase activity of EhHsp90. The Aha1 protein is characterized by the presence of two domains joined by a small linker, interaction analysis with the enzyme, overview 734478 3.6.4.10 geranylgeraniol presence of peptide NRLLLTG eliminates stimulatory effect 684406 3.6.4.10 goniothalamin a naturally occurring styryl-lactone, isolated from the air-dried bark of Goniothalamus tapis Miq., that increases both Km and kcat of Hsp90, it binds to the N-terminal domain of Hsp90 activates its ATPase activity, while inhibiting the chaperone function of Hsp90 734112 3.6.4.10 goniothalamin a naturally occurring styryl-lactone, that increases both Km and kcat of Hsp90. Goniothalamin binds to the N-terminal domain of HtpG. Goniothalamin does not influence the interaction of HtpG with a non-native protein or the anti-aggregation activity of HtpG significantly. But it inhibits the activity of HtpG that assists refolding of a non-native protein in cooperation with the Hsp70 chaperone system. Domain competition in presence of goniothalamin, overview. The N-terminal domain inhibits the enhancement of the activity by goniothalamin, whereas HtpG lacking the N-terminal domain, i.e. the middle domain fused to the C-terminal domain, does not affect the enhancement 734112 3.6.4.10 goniothalamin enhances the ATPase activity of the molecular chaperone Hsp90 (1.56fold at 0.04 mg/ml) 757111 3.6.4.10 goniothalamin enhances the ATPase activity of the molecular chaperone Hsp90 (1.76fold at 0.04 mg/ml) 757111 3.6.4.10 GroES required for the functioning of the Escherichia coli heat shock protein, also stimulates the reassembly 210499 3.6.4.10 GrpE - 210513 3.6.4.10 GrpE co-chaperone GrpE stimulates nucleotide exchange 80000fold 656484 3.6.4.10 GrpE heat shock protein, cochaperonin, increases effectiveness of DnaK 40fold 210505, 210509 3.6.4.10 Hch1p - 757741 3.6.4.10 Hep1 Hsp70 escort protein, interacts with mtHsp70 and is crucial for maintaining native mtHsp70 in its functional state, Hep1 is required for the folding of the ATPase domain of mtHsp70. Folding of mtHsp70 is impaired in mitochondria lacking Hep1 734351 3.6.4.10 Hsc20 cochaperone to Hsc66 210518 3.6.4.10 Hsc20 the ATPase activity of mtHSP70 is accelerated by co-chaperone HSC20 and further accelerated by HSC20 plus scaffold protein ISCU. mtHSP70 binds preferentially to the D-state of ISCU and that HSC20 binds preferentially to the S-state of ISCU 734233 3.6.4.10 HSP70 - 756406 3.6.4.10 ISCU the iron-sulfur cluster scaffold protein, the ATPase activity of mtHSP70 is accelerated by co-chaperone HSC20 and further accelerated by HSC20 plus scaffold protein ISCU. mtHSP70 binds preferentially to the D-state of ISCU and that HSC20 binds preferentially to the S-state of ISCU, detailed interaction analysis 734233 3.6.4.10 kappa-casein the enzyme exhibits a weak ATPase activity that is stimulated about 2fold by kappa-casein 758155 3.6.4.10 kappa-casein the enzyme exhibits a weak ATPase activity that is stimulated about 4fold by kappa-casein 758155 3.6.4.10 L-cysteine stimulates 2fold 669512 3.6.4.10 lambdaO - 210502 3.6.4.10 additional information aggregated glucose-6-phosphate dehydrogenase does not significantly affect the ATPase activity of the enzyme 758155 3.6.4.10 additional information aggregates of carboxymethylated alpha-lactalbumin, fluorescein-CALLQSRLLLSAPRRAAATAR, NRLLLTG, and tryptic fragments of casein smaller than 10 kDa fail to stimulate the DnaK-ClpB complex activity 758438 3.6.4.10 additional information deletion of the N-terminal domain activates the basal activity 2fold, whereas elimination of the M domain increases the ATPase activity 10fold in the presence of casein 733304 3.6.4.10 additional information mechanism of ClpB activation by comparing ATPase mechanisms and cryo-EM structures of ClpB wild-type and a constitutively active ClpB M-domain mutant. ClpB activation requires two signals: (1) interaction with the Hsp70 partner chaperone and (2) binding to substrate protein 756406 3.6.4.10 Nonidet P-40 - 210517 3.6.4.10 NRLLLTG peptide binding to the substrate-binding site. Stimulates ATPase activity, eliminates stimulatory effect of geranylgeraniol 684406 3.6.4.10 poly-L-lysine the enzyme exhibits a weak ATPase activity that is stimulated about 10fold by poly-L-lysine 758155 3.6.4.10 poly-L-lysine the enzyme exhibits a weak ATPase activity that is stimulated about 5fold by poly-L-lysine 758155 3.6.4.10 polylysine - 733263 3.6.4.10 tamoxifen a small molecule activator 734112 3.6.4.10 unfolded protein reduced carboxymethylated alpha-lactalbumin, 0.08 mM, 28% stimulation above intrinsic activity 656392