Binding of magnesium in a mutant Escherichia coli alkaline phosphatase changes the rate-determining step in the reaction mechanism

Biochemistry ◽  
1993 ◽  
Vol 32 (40) ◽  
pp. 10683-10691 ◽  
Author(s):  
Xu Xu ◽  
Evan R. Kantrowitz
Keyword(s):  
Escherichia Coli ◽  
Alkaline Phosphatase ◽  
Reaction Mechanism ◽  
Rate Determining Step

Full Kinetics and a Mechanism Investigation for the Generation of 4- Substituted 1, 4-Dihydropyridine Derivatives in the Presence of Green Catalyst and Aqueous Medium: Experimental Procedure

2020 ◽  
Vol 17 ◽  
Author(s):  
Sayyed Mostafa Habibi-Khorassani ◽  
Mehdi Shahraki ◽  
Sadegh Talaiefar
Keyword(s):  
Reaction Mechanism ◽  
Reaction Centre ◽  
Green Catalyst ◽  
Experimental Procedure ◽  
Dominant Mechanism ◽  
Rate Determining Step ◽  
12 Steps ◽  
Reaction Constant ◽  
Substituted 1 ◽  
Dihydropyridine Derivatives

Aims and Objective: The main objective of the kinetic investigation of the reaction among ethyl acetoacetate 1, ammoniumacetat 2, dimedone 3 and diverse substitutions of benzaldehyde 4-X, (X= H, NO2, CN, CF3, Cl, CH (CH3)2, CH3, OCH3, OCH3, and OH) for the generation of 4-substituted 1, 4-dihydropyridine derivatives (product 5) was the recognition of the most realistic reaction mechanism. The layout of the reaction mechanism studied kinetically by means of the UV-visible spectrophotometry approach. Materials and Methods: Among the various mechanisms, only mechanism1 (path1) involving 12 steps was recognized as a dominant mechanism (path1). Herein, the reaction between reactants 1 and 2 (kobs= 814.04 M-1 .min-1 ) and also compound 3 and 4-H (kobs= 151.18 M-1 .min-1 ) were the logical possibilities for the first and second fast steps (step1 and step2, respectively). Amongst the remaining steps, only step9 of the dominant mechanism (path1) had substituent groups (X) near the reaction centre that could be directly resonated with it. Results and Discussion: Para electron-withdrawing or donating groups on the compound 4-X increases the rate of the reaction 4 times more or decreases 8.7 times less than the benzaldehyde alone. So, this step is sensitive for monitoring any small or huge changes in the reaction rate. For this reason, step9 is the rate-determining step of the reaction mechanism (path1). Conclusion: The recent result is the agreement with the Hammett description with an excellent dual substituent factor (r = 0.990) and positive value of reaction constant (ρ = +0.9502) which confirmed both the resonance and inductive effects “altogether” contributed on the reaction centre of step9 in the dominant mechanism (path1).

3-D structure of the D153G mutant of Escherichia coli alkaline phosphatase: an enzyme with weaker magnesium binding and increased catalytic activity

1995 ◽  
Vol 8 (9) ◽  
pp. 865-871 ◽  
Author(s):  
Chris G. Dealwis ◽  
Liqing Chen ◽  
Catherine Brennan ◽  
Wlodek Mandecki ◽  
Cele Abad-Zapatero
Keyword(s):  
Escherichia Coli ◽  
Alkaline Phosphatase ◽  
Catalytic Activity ◽  
Magnesium Binding

scholarly journals The Reversible Dissociation of the Alkaline Phosphatase of Escherichia coli

1965 ◽  
Vol 240 (11) ◽  
pp. 4284-4292 ◽  
Author(s):  
Milton J. Schlesinger ◽  
Kathleen Barrett
Keyword(s):  
Escherichia Coli ◽  
Alkaline Phosphatase ◽  
Reversible Dissociation

scholarly journals The Reversible Dissociation of the Alkaline Phosphatase of Escherichia coli

1965 ◽  
Vol 240 (11) ◽  
pp. 4293-4298 ◽  
Author(s):  
Milton J. Schlesinger
Keyword(s):  
Escherichia Coli ◽  
Alkaline Phosphatase ◽  
Reversible Dissociation

scholarly journals Dephosphorylation of phosphoproteins by Escherichia coli alkaline phosphatase.

1977 ◽  
Vol 252 (17) ◽  
pp. 6082-6089 ◽  
Author(s):  
R L Mellgren ◽  
G R Slaughter ◽  
J A Thomas
Keyword(s):  
Escherichia Coli ◽  
Alkaline Phosphatase

scholarly journals A Study of the Substrate Specificity and Other Properties of the Alkaline Phosphatase of Escherichia coli

1962 ◽  
Vol 237 (3) ◽  
pp. 841-846 ◽  
Author(s):  
Leon A. Heppel ◽  
D.R. Harkness ◽  
R.J. Hilmoe
Keyword(s):  
Escherichia Coli ◽  
Alkaline Phosphatase ◽  
Substrate Specificity

scholarly journals Activation of a Mutationally Altered Form of the Escherichia coli Alkaline Phosphatase by Zinc

1966 ◽  
Vol 241 (13) ◽  
pp. 3181-3188
Author(s):  
Milton J. Schlesinger
Keyword(s):  
Escherichia Coli ◽  
Alkaline Phosphatase ◽  
Altered Form

scholarly journals A Mutationally Altered Alkaline Phosphatase from Escherichia coli

1972 ◽  
Vol 247 (7) ◽  
pp. 2087-2094
Author(s):  
Stephen E. Halford ◽  
David A. Lennette ◽  
Philip M. Kelley ◽  
Milton J. Schlesinger
Keyword(s):  
Escherichia Coli ◽  
Alkaline Phosphatase
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