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. 2011 Jul 18;286(37):32586–32592. doi: 10.1074/jbc.M111.251041

TABLE 1.

Kinetic constants for CapD, CP, and F24H

Each reaction was carried out with three independent measurements as described under “Experimental Procedures.” The errors represent the 95% confidence interval determined from nonlinear regression fit of the data. No product inhibition was observed for the transpeptidation reaction and was fit to Equation 1, whereas product inhibition was observed for the hydrolysis reaction and was fit to Equation 2. Error in kcat/Km was calculated using δ(kcat/Km) = |kcat/Km| δ(kcat/kcat)2+δ(Km/Km)2. NA, not applicable.

Transpeptidation Hydrolysis
CapD
    kcat (h−1) 68.07 ± 1.34 3.16 ± 0.31
    Km (nm) 65.45 ± 4.65 3.04 ± 1.00
    Ki (nm) NA 377.59 ± 126.48
    kcat/Km (m−1 s−1 × 103) 288.90 ± 21.30 288.74 ± 99.11

CP
    kcat (h−1) 63.37 ± 2.67 3.33 ± 0.35
    Km (nm) 43.72 ± 7.20 2.83 ± 1.00
    Ki (nm) NA 319.46 ± 112.35
    kcat/Km (m−1 s−1 × 103) 402.63 ± 6.84 326.86 ± 120.50

F24H
    kcat (h−1) 4.42 ± 0.20 1.72 ± 0.04
    Km (nm) 57.49 ± 9.54 6.92 ± 0.58
    Ki (nm) NA 3583.2 ± 726.98
    kcat/Km (m−1 s−1 × 103) 21.36 ± 3.67 69.04 ± 6.00