| Value |
2
µmol/liter
|
| Organism |
Unspecified |
| Reference |
Bernstein BW, Bamburg JR. Actin-ATP hydrolysis is a major energy drain for neurons. J Neurosci. 2003 Jan 1 23(1):1-6. p.4 right column bottom paragraphPubMed ID12514193
|
| Primary Source |
Zigmond SH (1993) Recent quantitative studies of actin filament turnover during cell locomotion. Cell Motil Cytoskel 25: 309–316. & Didry D, Carlier MF, PantaloniD (1998) Synergy between actin depolymerizing factor/cofilin and profilin in increasing actin filament turnover. J Biol Chem 273: 25602–25611.PubMed ID8402952, 9748225
|
| Comments |
"The actin treadmilling rate in cells is ~20 sec^-1, assuming that it is 200 times faster than the in vitro rate of 0.1 sec^-1 (1st primary source), i.e., there is a release of 20 subunits per pointed end per second (2nd primary source). Because
the rate-limiting step for actin-associated ATP hydrolysis is the
subunit release rate, a concentration of filament ends of 2µmol/l is required for 20 subunits per pointed end per second for the degradation of 40µmol ATP/liter/sec." |
| Entered by |
Uri M |
| ID |
110644 |