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Table 1 Substrate specificity of recombinant LcBADH1 and LcBADH2 proteins

From: Functional and expression analyses of two kinds of betaine aldehyde dehydrogenases in a glycinebetaine-hyperaccumulating graminaceous halophyte, Leymus chinensis

		LcBADH1			LcBADH2
Substrates	K _m (μM)	V _max (U mg ^-1 protein)	V _max / K _m	K _m (μM)	V _max (U mg ^-1 protein)	V _max / K _m
Betaine aldehyde	27300 ± 7000	1.59 ± 0.16	5.96 × 10⁻⁵ ± 1.22 × 10⁻⁵	109 ± 10.0	1.26 ± 0.05	1.16 × 10⁻² ± 1.55 × 10⁻⁴
AB-ald	48.1 ± 12.6	1.29 ± 0.08	3.55 × 10⁻² ± 1.28 × 10⁻²	1.96 ± 0.30	1.01 ± 0.04	5.17 × 10⁻¹ ± 3.27 × 10⁻²
AP-ald	27.4 ± 6.30	2.16 ± 0.14	1.03 × 10⁻¹ ± 3.10 × 10⁻²	4.53 ± 0.81	2.70 ± 0.17	5.96 × 10⁻¹ ± 2.85 × 10⁻²
TMAB-ald	56.5 ± 17.0	1.33 ± 0.19	2.91 × 10⁻² ± 5.69 × 10⁻³	22.1 ± 1.50	1.10 ± 0.02	5.03 × 10⁻² ± 4.18 × 10⁻³
TMAP-ald	762 ± 175	1.01 ± 0.08	1.22 × 10⁻³ ± 1.95 × 10⁻⁴	91.4 ± 9.60	1.81 ± 0.07	2.00 × 10⁻² ± 4.14 × 10⁻⁴
NAD⁺	15.6 ± 5.70	1.36 ± 0.12	1.11 × 10⁻¹ ± 3.69 × 10⁻²	7.66 ± 0.60	0.683 ± 0.01	9.02 × 10⁻² ± 9.34 × 10⁻³
NADP⁺		N.D.		3680 ± 725	0.273 ± 0.02	7.60 × 10⁻⁵ ± 8.29 × 10⁻⁶

For kinetic analyses of the substrates, reaction mixtures contained 50 mM HEPES-KOH (pH 8.0), 500 μM NAD⁺ and various concentrations of each substrates. For kinetic analyses of NAD⁺ and NADP⁺, reaction mixtures contained 50 mM HEPES-KOH (pH 8.0), betaine aldehyde (5 mM for LcBADH1; 200 μM for LcBADH2) and the various concentrations of NAD⁺ or NADP⁺. Enzyme activities were determined as described in Materials and Methods. Values represent the mean of three experiments ± SE. AB-ald, 4-aminobutyraldehyde; AP-ald, 3-aminopropionaldehyde; TMAB-ald, 4-N-trimethylaminobutyraldehyde; TMAP-ald, 3-N-trimethylaminopropionaldehyde. N.D.; not detected.

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