. 1999 Nov;121(3):913–919. doi: 10.1104/pp.121.3.913

Table I.

Kinetic and equilibrium constants of control and R286L ACC synthase

Enzyme	K_{m SAM}	k_cat	k_cat/K_{m SAM}	K_{D PLP}
Enzyme	K_{m SAM}	k_cat	k_cat/K_{m SAM}	25°C	35°C
	mm	s⁻¹	m⁻¹ s⁻¹	μm
Control (del-1)	0.12^a	9.79	8.15 × 10⁴	0.53^b	0.63^b
R286L	0.75^a	8.20 × 10⁻³	1.09 × 10	1.08 × 10^b	1.61 × 10^b
Control/R286L	0.16	1.20 × 10³	7.49 × 10³	4.9 × 10⁻²	3.9 × 10⁻²

Kinetic data were collected at pH 9.5 with a fixed PLP concentration of 500 μm and a variable AdoMet concentration from 20 to 2,000 μm.

The dissociation constants for the ACC synthase-PLP complex were determined based on data obtained from the fluorescence spectroscopic measurements at pH 7.5.