Effects of Acetyl CoA on the Pre-Steady-State Kinetics of the Biotin Carboxylation Reaction of Pyruvate Carboxylase†

Biochemistry ◽  
1996 ◽  
Vol 35 (12) ◽  
pp. 3849-3856 ◽  
Author(s):  
Glen B. Legge ◽  
Joy P. Branson ◽  
Paul V. Attwood
1991 ◽  
Vol 69 (9) ◽  
pp. 630-634
Author(s):  
M. James C. Crabbe ◽  
Derek Goode

Steady-state kinetic analysis of chloramphenicol acetyltransferase showed that medium effects (higher temperatures or pH, higher ionic strengths, or lower values for dielectric constant) altered the kinetic behaviour of the enzyme with acetyl-CoA as substrate, but did not significantly affect behaviour with chloramphenicol. This was manifest as an increase in the degree of the rate equation to a 2:2 function. This is interpreted in terms of perturbations to the enzyme at or near the acetyl-CoA binding region of the enzyme.Key words: acetyl coenzyme A, chloramphenicol, antibiotics, enzyme kinetics.


1978 ◽  
Vol 24 (3) ◽  
pp. 324-332 ◽  
Author(s):  
J. Bruni ◽  
B. J. Wilder ◽  
L. J. Willmore ◽  
R. J. Perchalski ◽  
H. J. Villarreal

1988 ◽  
Vol 66 (6) ◽  
pp. 250-256 ◽  
Author(s):  
G. Neugebauer ◽  
D. Platt ◽  
T. Vömel ◽  
W. Lösch

1990 ◽  
Vol 193 (3) ◽  
pp. 879-886 ◽  
Author(s):  
Heinrich STROTMANN ◽  
Renate THELEN ◽  
Wolfgang MULLER ◽  
Wolfgang BAUM

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