. 2013 Dec 24;70(Pt 1):79–90. doi: 10.1107/S1399004713024838

Table 1. Kinetic parameters (K _m, k _cat and k _cat/K _m) of AlrV and BsrV for various amounts (1.25–60 mM) of L-amino-acid substrates were calculated using data obtained with 0.47 µM purified racemase (see §2).

All kinetic constants must be considered as apparent values because of the impossibility of calculating initial enzyme velocities. The results are means ± SD of triplicates from two independent experiments. BsrV reaction kinetics for His and Cys were not determined (ND).

	K _m (mM)	k _cat (s⁻¹)	k _cat/K _m (mM ⁻¹ s⁻¹)
BrsV
Ala	11 ± 2	1.68 ± 0.11	15.3 × 10⁻²
Ser	28 ± 3	4.68 ± 0.21	16.7 × 10⁻²
Met	11 ± 2	2.94 ± 0.04	26.7 × 10⁻²
Leu	30 ± 7	2.30 ± 0.28	7.7 × 10⁻²
Cys	ND	ND	ND
Gln	22 ± 3	2.59 ± 0.16	11.8 × 10⁻²
Asn	15 ± 4	0.05 ± 0.004	0.3 × 10⁻²
His	ND	ND	ND
Lys	9 ± 1	4.76 ± 0.11	52.9
Arg	18 ± 3	5.09 ± 0.11	28.3
AlrV
Ala	1.5 ± 0.6	1.42 ± 0.003	94.5
Ser	17 ± 8	1.16 ± 0.0002	6.8

Table 1. Kinetic parameters (K m, k cat and k cat/K m) of AlrV and BsrV for various amounts (1.25–60 mM) of L-amino-acid substrates were calculated using data obtained with 0.47 µM purified racemase (see §2).

Table 1. Kinetic parameters (K _m, k _cat and k _cat/K _m) of AlrV and BsrV for various amounts (1.25–60 mM) of L-amino-acid substrates were calculated using data obtained with 0.47 µM purified racemase (see §2).