EC Number |
Activating Compound |
Reference |
---|
7.4.2.3 | DnaJ |
bacterial co-chaperone stimulates ATPase activity of mtHsp70 5fold, that of DnaK 20fold |
668549 |
7.4.2.3 | fluorescein-CALLQSRLLLSAPRRAAATARY |
similar affininty of mtHsp70 and Dnak at 25°C |
668549 |
7.4.2.3 | GrpE |
bacterial co-chaperone stimulates ATPase activity of mtHsp70 5fold, that of DnaK 20fold |
668549 |
7.4.2.3 | GrpEL1 |
the proposed nucleotide exchange factor of the human mtHsp70 machine. To access the nucleotide relase of human GrpEL1, a single turnover ATPase assay is performed to monitor the hydrolysis of the prebound mtHsp70-ATP complex of the wild-type protein in the presence of GrpEL1. Human GrpEL1 shows robust nucleotide exchange activity in the presence of excess unlabeled ATP, thus inhibiting the maximum ATP hydrolysis of wild-type mtHsp70 |
712438 |
7.4.2.3 | H2O2 |
stimulates association of mtHsp70 with wild-type DJ-1 |
673805 |
7.4.2.3 | Hsp40-related J domain protein DJA1 |
- |
688903 |
7.4.2.3 | Hsp40-related J domain protein DJA2 |
- |
688903 |
7.4.2.3 | Hsp40-related J domain protein DJA4 |
- |
688903 |
7.4.2.3 | human escort protein |
Hep, stimulates the activity of mtHsp70 49fold, and also 11.5fold the activity of the isolated ATPase domain. Hep binding to full-length mtHsp70 and its isolated ATPase domain is strongest in the absence of nucleotides |
698800 |
7.4.2.3 | human Hsp70 escort protein |
human Hsp70 escort protein (Hep) possesses the unique ability to stimulate the ATPase activity of mtHsp70 as well as to prevent the aggregation of unfolded client proteins similar to J-proteins |
712438 |