. Author manuscript; available in PMC: 2015 Apr 24.

Published in final edited form as: Chem Biol Interact. 2011 Jan 20;191(0):278–287. doi: 10.1016/j.cbi.2011.01.013

Table 1.

Kinetic properties of recombinant mouse Aldhs

	Aldh1a1			Aldh3a1

Substrate	V_max^a	K_m^b	V_max/K_m^c	V_max^d	K_m^b	V_max/K_m^c
Propionaldehyde	799 ± 22	141 ± 30	5.6	24.7 ± 1.2	3380 ± 38	7
Acetaldehyde	910 ± 36	202 ± 17	4.5	32.4 ± 1.0	1000 ± 20	32
Benzaldehyde	256 ± 14	752 ± 90	0.3	28.6 ± 1.6	37 ± 6	773
Trans-2-hexenal	390 ± 37	31.2 ± 4.1	12.5	28.1 ± 1.1	236 ± 40	119
HNE	522 ± 26	2.4 ± 0.9	218	29.5 ± 3.7	425 ± 94	69
Acrolein	527 ± 22	23.2 ± 4.3	23	10.8 ± 1.1	464 ± 85	23
Malondialdehyde	408 ± 15	7.5 ± 1.2	54	8.3 ± 0.7	302 ± 52	27
NAD⁺	751 ± 7	50.2 ± 4	15	26.9 ± 5.9	55.5 ± 2.3	484
NADP⁺	0	0	0	28 ± 7.5	320 ± 18	87

Aldh enzyme activity was determined by monitoring the formation of NADH at 340 nm. Enzyme activities were measured spectrophotometrically at 25°C in a reaction mixture containing 1 mM NAD⁺ at pH 7.4. The kinetic parameters were determined using non-linear regression software Kineti77. The values represent the means ± SD from 3–4 assays. The kinetic parameters for NAD⁺ and NADP⁺ were determined using 1 mM propionaldehyde (Aldh1a1) or 2.5 mM benzaldehyde (Aldh3a1) as the substrate.

V_max values are expressed as nmol of NADH/min/mg of protein

K_m are expressed in μM

V_max/K_m values are expressed as ml/min/mg (after normalization of V_max to μmol product/min/mg)

V_max is expressed in μmol/min/mg