Chorismate synthase. Pre-steady-state kinetics of phosphate release from 5-enolpyruvylshikimate 3-phosphate.
The pre-steady-state kinetics of phosphate formation from 5-enolpyruvylshikimate 3-phosphate catalysed by Escherichia coli chorismate synthase (EC 4.6.1.4) were studied by a rapid-acid-quench technique at 25 degrees C at pH 7.5. No pre-steady-state 'burst' or 'lag' phase was observed, showing that phosphate is released concomitant with the rate-limiting step of the enzyme. The implications of this result for the mechanism of action of chorismate synthase are discussed.
Hawkes
T R
TR
I.C.I. Agrochemical, Jcalotts Hill Research Station, Bracknell, Berks, U.K.
Lewis
T
T
Coggins
J R
JR
Mousdale
D M
DM
Lowe
D J
DJ
Thorneley
R N
RN
D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D004926:Escherichia coli / Q000201:enzymology; D007700:Kinetics; D008190:Lyases / Q000378:metabolism*; D010710:Phosphates / Q000378:metabolism*; D019761:Phosphorus-Oxygen Lyases; D012765:Shikimic Acid / Q000031:analogs & derivatives* / Q000378:metabolism
D010710:Phosphates; C058070:5-enolpyruvoylshikimate-3-phosphate; D012765:Shikimic Acid; D008190:Lyases; C019895:chorismate synthase; D019761:Phosphorus-Oxygen Lyases