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. Author manuscript; available in PMC: 2010 Sep 18.
Published in final edited form as: Biochem Biophys Res Commun. 2009 Jun 27;387(2):245–250. doi: 10.1016/j.bbrc.2009.06.123

Table 1. Kinetic parameters of AKR1B10 to carbonyls and glutathione conjugates.

AKR1B10 activity was measured as described in Materials and Methods. Constants were calculated by a Lineweaver-Burk plot of the reduction rate at various substrate concentrations. Vmax is expressed at nmol/mg protein/min. GS, glutathione; ND, not detectable; Cn, carbon chain length.

AKR1B10

Substrates Cn Vmax
(nmol/mg/min)
Km
(µM)
kcat
(min−1)
kcat/Km
(min−1 µM−1)
Acrolein a 3 3,122.0 ± 64.7 110.1 ± 12.2 115.9 ± 7.8 1.07
Crotonaldehyde a 4 2,647.5 ± 132.2 86.7 ± 14.3 103.4 ± 3.5 1.20
Trans-2-hexanal 6 2,658.1 ± 222.8 60.6 ± 18.5 97.4 ± 8.0 1.62
Trans-2, 4-hexadienal 6 2,160.8 ± 310.6 95.7 ± 5.6 82.8 ± 7.4 0.87
4-Hydroxynonenal 9 3,298.7 ± 245.9 30.9 ± 7.1 120.7 ± 6.5 3.92
GS-acrolein 64.36 ± 5.6 532.8 ± 70.6 2.8 ± 0.1 0.005
GS-crotonaldehyde 1,900.7 ± 90.9 245.7 ± 21.2 70.2 ± 3.5 0.29
GS-trans-2-hexanal 2,049.0 ± 116.3 145.7 ± 20.5 71.3 ± 2.6 0.51
GS-trans-2, 4-hexadienal 4,004.1 ± 362.5 77.6 ± 19.2 147.1 ± 10.1 1.91
GS-4-hydroxynonenal ND ND ND ND
a

Reference [13]