| Value |
110
ATP/min/26S
Range: ±12 ATP/min/26S
|
| Organism |
Budding yeast Saccharomyces cerevisiae |
| Reference |
Henderson A, Erales J, Hoyt MA, Coffino P. Dependence of proteasome processing rate on substrate unfolding. J Biol Chem. 2011 May 20 286(20):17495-502. doi: 10.1074/jbc.M110.212027 abstract and p.17499 left column bottom paragraph & p.17500 table 2 & p.17501 left column bottom paragraphPubMed ID21454622
|
| Method |
"The ATPase activity reported as number of ATP molecules hydrolyzed per min
per doubly-capped 26S proteasome particle...Proteasome ATPase activity was measured
in a coupled assay (19, 20) in 25 mM HEPES (pH 7.5), 100 mM
KCl, 20 mM MgCl2, 10% glycerol, 250 mU/ml LDH/pyruvate
kinase (Sigma), 7.5 mM phospho(enol)pyruvic acid, 1 mM
NADH, 2mM DTT, and 5mM ATP." |
| Comments |
"ATP turnover was
110/min./proteasome, and was not markedly changed by substrate...The rate of ATP
turnover was 110/proteasome/min. and varied modestly
among several independently prepared lots." |
| Entered by |
Uri M |
| ID |
109936 |