TABLE 1.

Steady-state kinetic parameters for vanillyl-alcohol oxidase from P. simplicissimum^a

Substrate	Km (μM)	kcat (s−1)	kcat/Km (103 s−1 M−1)
4-Ethylphenolb	9	2.5	280
4-n-Propylphenolb	4	4.2	1,050
2-Methoxy-4-n-propylphenolb	6	4.9	820
4-Isopropylphenol	16	1.3	81
4-sec-Butylphenol	72	0.5	7
4-n-Butylphenol	2	1.2	600
4-n-Pentylphenol	8	0.3	38
4-n-Heptylphenol	42	<0.001	<0.02
4-(3′-Methylcrotyl)phenol	65	1.4	21
1-(4′-Hydroxyphenyl)-2-butanone	128	0.3	2
5-Indanol	77	0.5	7
5,6,7,8-Tetrahydro-2-naphthol	94	0.7	7
(R,S)-1-(4′-Hydroxyphenyl)propanol	30	3.0	100
(R)-1-(4′-Hydroxyphenyl)ethanol	222	0.7	3
(S)-1-(4′-Hydroxyphenyl)ethanol	26	4.4	170
2-(4′-Hydroxyphenyl)ethanol	100	0.004	0.04
3-(4′-Hydroxyphenyl)propanol	8	0.1	13

^aStandard errors of kinetic parameters were less than 10% except for 4-n-heptylphenol and 2-(4′-hydroxyphenyl)ethanol, which had standard errors of about 25%. 

^bData from Drijfhout et al. (3).