Catalysis of tRNA Aminoacylation: Single Turnover to Steady-State Kinetics of tRNA Synthetases

2012 ◽  
Vol 116 (39) ◽  
pp. 11809-11817 ◽  
Author(s):  
Mantu Santra ◽  
Biman Bagchi
1985 ◽  
Vol 231 (1) ◽  
pp. 83-88 ◽  
Author(s):  
R Bicknell ◽  
S G Waley

The kinetics of the hydrolysis of two cephalosporins by β-lactamase I from Bacillus cereus 569/H/9 has been studied by single-turnover and steady-state methods. Single-turnover kinetics could be measured over the time scale of minutes when cephalosporin C was the substrate. The other substrate, 7-(2′,4′-dinitrophenylamino)deacetoxycephalosporanic acid, was hydrolysed even more slowly, and has potential for use in crystallographic studies of β-lactamases. Comparison of single-turnover and steady-state kinetics showed that, for both substrates, opening the β-lactam ring (i.e. acylation of the enzyme) was the rate-determining step. Thus the non-covalent enzyme-substrate complex is expected to be the intermediate observed crystallographically.


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

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