. 2005 Feb 8;386(Pt 1):57–62. doi: 10.1042/BJ20040490

Table 1. Steady-state kinetic parameters for His₆–PimD and other macrolide oxidases.

Enzyme	Substrate	k_cat (s⁻¹)	K_m (μM)	K_cat/K_m (μM⁻¹·s⁻¹)	Source
PimD	4,5-De-epoxypimaricin	1.5±0.34	93±29	0.016±0.002	This work
PimD^*	4,5-De-epoxypimaricin	0.78±0.04	33±5.5	0.024±0.003	This work
EryF	6-Deoxyerythronolide B	1.7	1.98±0.26	0.85±0.11	[16]
EryK	Erythromycin D	6.2±1.2	44±10	0.14±0.042	[17]
EryK^*	Erythromycin D	1.8±0.18	8±2.3	0.22±0.068	[17]
PicK	YC-17	1.1±0.08	130±20	0.008±0.004	[18]
PicK	Narbomycin	2.0±0.3	88±24	0.023±0.01	[18]
PicK^*	YC-17	0.6±0.05	20.4±5.6	0.029±0.008	[7]
PicK^*	Narbomycin	1.0±0.11	43.7±5.9	0.023±0.018	[7]

* Apparent values obtained from fitting the Michaelis–Menten equation to the low-concentration data in the linear region of the saturation curve.

Table 1. Steady-state kinetic parameters for His6–PimD and other macrolide oxidases.