| Value |
50
Sec^-1
|
| Organism |
Bacteria Bacillus subtilis |
| Reference |
Mattei P, Kast P, Hilvert D. Bacillus subtilis chorismate mutase is partially diffusion-controlled. Eur J Biochem. 1999 Apr261(1):25-32. p.26 left column top paragraphPubMed ID10103029
|
| Primary Source |
Gray JV, Eren D, Knowles JR. Monofunctional chorismate mutase from Bacillus subtilis: kinetic and 13C NMR studies on the interactions of the enzyme with its ligands. Biochemistry. 1990 Sep 18 29(37):8872-8.PubMed ID2125470
|
| Comments |
"In
the case of the structurally distinctive BsCM, product dissociation
has been proposed to be limiting under saturating
conditions due to the coincidence of the rate constant for the
dissociation of prephenate obtained from line-broadening
experiments (~60s^-1 at 30°C) and the turnover number for
the enzyme determined kinetically (50 s^-1) [primary source]." |
| Entered by |
Uri M |
| ID |
109299 |