Overexpression, Purification, and Characterization of Escherichia coli Acyl Carrier Protein and 2 Mutant Proteins

1995 ◽  
Vol 6 (4) ◽  
pp. 394-400 ◽  
Author(s):  
R.B. Hill ◽  
K.R. Mackenzie ◽  
J.M. Flanagan ◽  
J.E. Cronan ◽  
J.H. Prestegard
Keyword(s):  
Escherichia Coli ◽  
Acyl Carrier Protein ◽  
Carrier Protein ◽  
Purification And Characterization ◽  
Mutant Proteins

Purification and characterization of Rhodobacter sphaeroides acyl carrier protein

Biochemistry ◽  
1987 ◽  
Vol 26 (10) ◽  
pp. 2740-2746 ◽  
Author(s):  
Cynthia L. Cooper ◽  
Stephen G. Boyce ◽  
Donald R. Lueking
Keyword(s):  
Rhodobacter Sphaeroides ◽  
Acyl Carrier Protein ◽  
Carrier Protein ◽  
Purification And Characterization

scholarly journals Purification and characterization of [acyl-carrier-protein] acetyltransferase from Escherichia coli

1988 ◽  
Vol 250 (3) ◽  
pp. 789-796 ◽  
Author(s):  
P N Lowe ◽  
S Rhodes
Keyword(s):  
Escherichia Coli ◽  
Acyl Carrier Protein ◽  
Carrier Protein ◽  
E Coli ◽  
Step Procedure ◽  
Ping Pong ◽  
Protein Acetyltransferase ◽  
Enzyme Intermediate ◽  
Specific Reagent

A multi-step procedure has been developed for the purification of [acyl-carrier-protein] acetyltransferase from Escherichia coli, which allows the production of small amounts of homogeneous enzyme. The subunit Mr was estimated to be 29,000 and the native Mr was estimated to be 61,000, suggesting a homodimeric structure. The catalytic properties of the enzyme are consistent with a Bi Bi Ping Pong mechanism and the existence of an acetyl-enzyme intermediate in the catalytic cycle. The enzyme was inhibited by N-ethylmaleimide and more slowly by iodoacetamide in reactions protected by the substrate, acetyl-CoA. However, the enzyme was apparently only weakly inhibited by the thiol-specific reagent methyl methanethiosulphonate. The nature of the acetyl-enzyme intermediate is discussed in relationship to that found in other similar enzymes from E. coli, yeast and vertebrates.

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