. 2013 May 14;25(5):1756–1773. doi: 10.1105/tpc.113.111393

Table 2. In Vitro MYR Assay of Various Peptides Using Recombinant Wild-Type NMT1 and NMT1A160T.

NMT1^a
Protein of Origin^b	Substrate Assayed	K_m (µM)	k_cat (s⁻¹)	k_cat/K_m (10³ M⁻¹⋅s⁻¹)
ARFA1adf	GLSFAKLFRR	29 ± 5	0.65 ± 0.03	21.9
TRXh2	GGALSTVF	60 ± 17	0.28 ± 0.03	4.6
TRXh7	GSNVSSVH	301 ± 41	0.26 ± 0.02	0.88
TRXh8	GANVSTPD	545 ± 159	0.55 ± 0.11	1.0
TRXh9	GGSCVSKGK	18 ± 3	0.027 ± 0.011	1.5
PLL5	GNGVTKLS	12 ± 4	0.15 ± 0.07	11.9
RPS5-like	GGCVSVQV	2.4 ± 0.4	0.075 ± 0.001	31.7
SOS3	GCSVSKKK	7.4 ± 2.2	0.091 ± 0.004	13.0
SOS3	Myr-CoA	1.7 ± 0.3	0.153 ± 0.007	89
NMT1A160T^a
Protein of Origin^b	Substrate Assayed	K_m (µM)	k_cat (s⁻¹)	k_cat/K_m (10³ M⁻¹⋅s⁻¹)	Reduction of k_cat/K_m (Fold versus Wild Type)
ARFA1adf	GLSFAKLFRR	68 ± 14	0.091 ± 0.006	1.3	16.5
TRXh2	GGALSTVF	197 ± 53	0.044 ± 0.001	0.22	21
TRXh7	GSNVSSVH	176 ± 54	0.05 ± 0.01	0.27	3.3
TRXh8	GANVSTPD	926 ± 301	0.18 ± 0.03	0.20	5
TRXh9	GGSCVSKGK	106 ± 28	0.029 ± 0.004	0.28	5.2
PLL5	GNGVTKLS	36 ± 2	0.028 ± 0.002	0.76	16
RPS5-like	GGCVSVQV	50 ± 8	0.034 ± 0.002	0.67	47
SOS3	GCSVSKKK	57 ± 11	0.069 ± 0.004	1.18	11
SOS3	Myr-CoA	38 ± 11	0.062 ± 0.007	1.63	54

Kinetic parameters obtained from an in vitro continuous fluorigenic NMT assay and several N-terminal peptides (Traverso et al., 2013a).

N-terminal octapeptides (from amino acids 2 to 9) were derived from Arabidopsis proteins for which MYR was previously predicted and/or reported (Traverso et al., 2013a, 2013b). The k_cat/K_m value reflects the catalytic efficiency of each peptide to be MYRed by the NMT enzyme.