Volume 451 (2013), pp. 205–216

The column for the kinetic parameters in Table 4 was omitted from the published article. The full Table appears here.

Table 4
Stopped-flow single turnover rates for R. capsulatus wild-type ALAS and the ALAS T83S variant with L-alanine or glycine

The R. capsulatus ALAS reaction was fitted to a four-step reaction with four observable rates. k1, rate of the formation of the initial collision complex; k2, rate of the formation of quinonoid intermediate I/II; k3, rate of the formation of the enzyme–product complex; k4, rate of the dissociation of the enzyme–product complex into the enzyme and product; k−1, decay of initial collision complex; k−2, decay of the quinonoid intermediates I/II; k−3, decay of the enzyme–product complex; k−4, reverse rate of the enzyme and product formation; ND, non-detectable under the experimental conditions.

EnzymeKinetic parameterGlycine (s−1)L-Alanine (s−1)
ALAS wild-type k1 ND ND 
 k2 ND ND 
 k3 ND ND 
 k4 ND ND 
 k−1 ND ND 
 k−2 ND ND 
 k−3 ND ND 
 k−4 ND ND 
T83S k1 0.17±4.64×10−5 2.77×10−2±9.01×10−9 
 k2 1.76±3.87×10−8 0.29±5.10×10−6 
 k3 2.39±8.86×10−10 0.39±1.19×10−7 
 k4 0.06±3.11×10−3 9.48×10−3±952.92 
 k−1 10.06±3.97×10−4 1.67±1.86×10−6 
 k−2 0.03±4.59×10−6 5.12×10−3±0.42 
 k−3 0.33±2.12×10−6 5.14×10−2±1.08×10−3 
 k−4 2.81×10−4±6.95×10−8 4.68×10−5±1.59×10−7 
EnzymeKinetic parameterGlycine (s−1)L-Alanine (s−1)
ALAS wild-type k1 ND ND 
 k2 ND ND 
 k3 ND ND 
 k4 ND ND 
 k−1 ND ND 
 k−2 ND ND 
 k−3 ND ND 
 k−4 ND ND 
T83S k1 0.17±4.64×10−5 2.77×10−2±9.01×10−9 
 k2 1.76±3.87×10−8 0.29±5.10×10−6 
 k3 2.39±8.86×10−10 0.39±1.19×10−7 
 k4 0.06±3.11×10−3 9.48×10−3±952.92 
 k−1 10.06±3.97×10−4 1.67±1.86×10−6 
 k−2 0.03±4.59×10−6 5.12×10−3±0.42 
 k−3 0.33±2.12×10−6 5.14×10−2±1.08×10−3 
 k−4 2.81×10−4±6.95×10−8 4.68×10−5±1.59×10−7 
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© The Authors Journal compilation © 2013 Biochemical Society
2013