Pre-steady-state kinetics of Escherichia coli aspartate aminotransferase catalyzed reactions and thermodynamic aspects of its substrate specificity

Biochemistry ◽  
1990 ◽  
Vol 29 (23) ◽  
pp. 5469-5476 ◽  
Author(s):  
Seiki Kuramitsu ◽  
Keitaro Hiromi ◽  
Hideyuki Hayashi ◽  
Yoshimasa Morino ◽  
Hiroyuki Kagamiyama
Keyword(s):  
Escherichia Coli ◽  
Steady State ◽  
Substrate Specificity ◽  
Aspartate Aminotransferase ◽  
Steady State Kinetics ◽  
Catalyzed Reactions ◽  
Kinetics Of

scholarly journals Chorismate synthase. Pre-steady-state kinetics of phosphate release from 5-enolpyruvylshikimate 3-phosphate

1990 ◽  
Vol 265 (3) ◽  
pp. 899-902 ◽  
Author(s):  
T R Hawkes ◽  
T Lewis ◽  
J R Coggins ◽  
D M Mousdale ◽  
D J Lowe ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Steady State ◽  
Lag Phase ◽  
Chorismate Synthase ◽  
Phosphate Release ◽  
Rate Limiting Step ◽  
Limiting Step ◽  
Steady State Kinetics ◽  
Rate Limiting ◽  
Kinetics Of

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.

scholarly journals Studies on alkaline phosphatase. Transientstate and steady-state kinetics of Escherichia coli alkaline phosphatase

1969 ◽  
Vol 111 (2) ◽  
pp. 187-194 ◽  
Author(s):  
H N Fernley ◽  
P. G. Walker
Keyword(s):  
Escherichia Coli ◽  
Alkaline Phosphatase ◽  
Steady State ◽  
Substrate Concentration ◽  
Marked Effect ◽  
Binding Constants ◽  
Transient State ◽  
Steady State Kinetics ◽  
Ph Range ◽  
Kinetics Of

1. The transient-state and steady-state phases of the reaction between Escherichia coli alkaline phosphatase and 4-methylumbelliferyl phosphate were investigated by using a fluorimetric stopped-flow technique. 2. At low substrate concentration (5μm) in the pH range 3·8–6·3 there was an initial rapid liberation of up to 1mole of 4-methylumbelliferone/mole of enzyme. 3. At very low substrate concentration (0·1μm) in the pH range 4·9–5·9 an initial lag in 4-methylumbelliferone production was observed, from which values for k+1 and k−1 could be obtained. 4. The pH profiles for the rates of phosphorylation and dephosphorylation are quite different, and it is postulated that an ionizing group which determines the conformation during the phosphorylation step is not involved in the dephosphorylation step. 5. The binding constants for substrate and Pi are similar throughout the pH range 4–8. The ionization of substrate or Pi appeared to have no marked effect on the binding.

Steady-state kinetics of valproic acid in epileptic patients

1978 ◽  
Vol 24 (3) ◽  
pp. 324-332 ◽  
Author(s):  
J. Bruni ◽  
B. J. Wilder ◽  
L. J. Willmore ◽  
R. J. Perchalski ◽  
H. J. Villarreal
Keyword(s):  
Valproic Acid ◽  
Steady State ◽  
Steady State Kinetics ◽  
Epileptic Patients ◽  
Kinetics Of
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