Catalytic mechanism of Escherichia coli alkaline phosphatase: resolution of three variants of the acyl-enzyme mechanism

Biochemistry ◽  
1980 ◽  
Vol 19 (22) ◽  
pp. 5008-5018 ◽  
Author(s):  
Will Bloch ◽  
Michael S. Gorby
Keyword(s):  
Escherichia Coli ◽  
Alkaline Phosphatase ◽  
Catalytic Mechanism ◽  
Enzyme Mechanism

scholarly journals Escherichia coli alkaline phosphatase. Relaxation spectra of ligand binding

1972 ◽  
Vol 126 (3) ◽  
pp. 727-738 ◽  
Author(s):  
S. E. Halford
Keyword(s):  
Escherichia Coli ◽  
Alkaline Phosphatase ◽  
Ligand Binding ◽  
Catalytic Mechanism ◽  
Temperature Jump ◽  
Relaxation Spectrum ◽  
Equilibrium Mixture ◽  
Difference Spectroscopy ◽  
Relaxation Spectra

The temperature-jump technique was used to study the binding equilibrium between the Escherichia coli alkaline phosphatase dimer and 2-hydroxy-5-nitrobenzyl phosphonate in 0.1m-tris buffer, pH8.0. Three partially discrete relaxations were observed, two of which could be related to the bimolecular associations of ligand with different conformations of the enzyme and the third to the interconversion of these states. Relaxation spectra were also used to analyse the changes in the mechanism of ligand binding to alkaline phosphatase caused by increase in ionic strength. The relaxation spectrum observed after the addition of Pi to the equilibrium mixture of phosphonate and enzyme was also studied. Difference spectroscopy indicated that both of these ligands were bound to the alkaline phosphatase dimer at the same time. These results are related to the catalytic mechanism of this enzyme, with particular reference to the role of two identical subunits in a dimeric enzyme that exhibits only one active site functioning in catalysis at any given time.

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 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
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