| Range |
ATP synthesis 82: ATP hydrolysis 425 sec^-1
|
| Organism |
Bacteria Escherichia coli |
| Reference |
Tomashek JJ, Glagoleva OB, Brusilow WS. The Escherichia coli F1F0 ATP synthase displays biphasic synthesis kinetics. J Biol Chem. 2004 Feb 6 279(6):4465-70 DOI: 10.1074/jbc.M310826200 p.4469 right column top paragraphPubMed ID14602713
|
| Primary Source |
[15] Al-Shawi MK, Ketchum CJ, Nakamoto RK. The Escherichia coli FOF1 gammaM23K uncoupling mutant has a higher K0.5 for Pi. Transition state analysis of this mutant and others reveals that synthesis and hydrolysis utilize the same kinetic pathway. Biochemistry. 1997 Oct 21 36(42):12961-9. DOI: 10.1021/bi971478rPubMed ID9335556
|
| Comments |
P.4469 right column top paragraph: "In comparison, Al-Shawi et al. (primary source) measured turnover numbers in wild type membranes of 82 sec^-1 for ATP synthesis in non-DCCD-treated membranes and 425 s^-1 for ATP hydrolysis." Primary source abstract: "Wild-type enzyme had a turnover number of 82 s^-1 at pH 7.5 and 30 degrees C." |
| Entered by |
Uri M |
| ID |
115179 |