Purification and characterization of a cytoplasmic enzyme component of the Na+-activated malonate decarboxylase system of Malonomonas rubra: acetyl-S-acyl carrier protein: malonate acyl carrier protein-SH transferase

1994 ◽  
Vol 162 (1-2) ◽  
pp. 48-56
Author(s):  
Hubert Hilbi ◽  
Peter Dimroth
Keyword(s):  
Acyl Carrier Protein ◽  
Carrier Protein ◽  
Purification And Characterization ◽  
Cytoplasmic Enzyme

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 The purification and characterization of acetoacetyl-coenzyme A reductase from Azotobacter beijerinckii

1971 ◽  
Vol 121 (2) ◽  
pp. 309-316 ◽  
Author(s):  
G. A. F. Ritchie ◽  
P. J. Senior ◽  
E. A. Dawes
Keyword(s):  
Substrate Specificity ◽  
Reaction Rate ◽  
Acyl Carrier Protein ◽  
Thiol Group ◽  
Carrier Protein ◽  
Purification And Characterization ◽  
Michaelis Constants ◽  
Coa Reductase ◽  
Acetoacetyl Coa Reductase

A soluble acetoacetyl-CoA reductase (EC 1.1.1.36) was purified 54-fold from Azotobacter beijerinckii N.C.I.B. 9067 and the reaction product identified as d(−)-β-hydroxybutyryl-CoA. The Michaelis constants for acetoacetyl-CoA, NADPH and NADH were determined and the reaction rate was found to be some fivefold greater with NADPH than with NADH. At neutral pH the equilibrium greatly favours the formation of the reduced product. Substrate specificity was in the order: acetoacetyl-CoA>acetoacetylpantetheine>acetoacetyl-(acyl-carrier protein). The enzyme possesses a functional thiol group, suffers inactivation by oxygen and is inhibited by thiol-blocking reagents. Inhibition by p-chloromercuribenzoate is reversed by excess of dithiothreitol, which also protects the enzyme from inactivation by oxygen.

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