. 2026 Mar 25;43(1):105–115. doi: 10.5511/plantbiotechnology.25.1209a

Table 2. Kinetic parameters of recombinant HvACT-2HS1 and HvACT-2HL1.

Substrate	HvACT-2HS1			HvACT-2HL1^c
Substrate	K_m (μM)	k_cat (s⁻¹)	k_cat/K_m (s⁻¹ μM⁻¹)	K_m (μM)	k_cat (s⁻¹)	k_cat/K_m (s⁻¹ μM⁻¹)
Acyl donors
p-Coumaroyl-CoA^a	6.5±1.8	8.2±0.92	1.3	1.1±0.12	39±1.0	35
Feruloyl-CoA^a	5.6±2.2	3.3±0.33	0.59	2.0±0.14	18±0.31	9.0
Acyl acceptors
Agmatine^b	24±2.1	8.7±0.34	0.36	1.7±0.13	38±0.87	22
Putrescine^b	24,000±4,700	0.19±0.021	0.0000079	7,200±530	4.7±0.12	0.00065

Data are presented as the mean±SEM (SEM: error in data fitting to the Michaelis–Menten equation as calculated by a non-linear fitting program). Michaelis–Menten plots for each analysis are presented in Supplementary Figure S8. ^a 100 µM agmatine as the acyl acceptor. ^b 100 µM p-coumaroyl-CoA as the acyl donor. ^c Data are from Nomura et al. (2018). Values for HvACT-2HS1 are different from those in Table 1. The data in this table are based on the enzyme reaction under the same conditions as those used for HvACT-2HL1 (Nomura et al. 2018). The data in Table 1 are based on the enzyme reaction under optimal conditions for HvACT-2HS1.