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Table 1 Kinetic parameters, Vmax and Km, of α-IPMS reacting to α-ketoisovaleric acid and acetyl CoAa

From: Characterization of α-isopropylmalate synthases containing different copy numbers of tandem repeats in Mycobacterium tuberculosis

α-IPMS

α-Ketoisovaleric acid

Acetyl CoA

 

Km

(μM)

Vmax

(U/mg protein)

R2

k cat b

(s-1)

k cat /Km

(s-1 M-1)

Km

(μM)

Vmax

(U/mg protein)

R2

k cat b

(s-1)

k cat /Km

(s-1 M-1)

α-IPMS-2CR

261

(S.E. = 14.7)

0.49

(S.E. = 0.01)

0.99

1.17

4480

568

(S.E. = 94.5)

0.93

(S.E. = 0.06)

0.99

2.22

3,900

α-IPMS-14CR

35

(S.E. = 5.4)

0.16

(S.E. = 0.01)

0.96

0.52

14,800

27

(S.E. = 6.9)

0.19

(S.E. = 0.01)

0.93

0.61

22,590

  1. a At pH 8.5 and 37°C. The apparent Km and Vmax values were determined by varying the concentrations of one substrate at a fixed saturating concentration of the other substrate. α-ketoisovaleric acid and acetyl CoA was fixed at 2 mM and 0.8 mM, respectively. Data are the average of two assays. Prism software (version 3.08) was used for nonlinear regression, curve fit analysis to calculate Km and Vmax.
  2. bk cat = Vmax/[E] (μmol s-1mg-1)/(mol mg-1)