Microbial Cell Factories

Table 4 Comparison of apparent kinetic constants of recombinant pyranose oxidase from Lyophyllum shimeji (Ls P2Ox), Trametes multicolor (Tm P2Ox) and Phanerochaete chrysosporium (Pc P2Ox) for the electron acceptor substrates ferrocenium ion (Fc⁺), 1,4-benzoquinone (BQ) and 2,6-dichloroindophenol (DCIP).

From: Characterisation of recombinant pyranose oxidase from the cultivated mycorrhizal basidiomycete Lyophyllum shimeji (hon-shimeji)

Enzyme		K_m [mM]	k_cat [s^-1]	k_cat/K_m [mM^-1s^-1]	rel. k_cat/K_m^a[%]
Ls P2Ox	Fc⁺	0.187	39.9	213	100
	BQ	0.033	92.3	2760	100
	DCIP	0.187	67.3	361	100
Tm P2Ox	Fc⁺	0.507	291	574	269
	BQ	0.253	225	895	32.4
	DCIP	0.413	42.0	102	28.2
Pc P2Ox	Fc⁺	0.330	228	691	324
	BQ^b	0.110	400	3640	132
	DCIP^b	0.051	108	2120	587

^acatalytic efficiency k_cat/K_m relative to the value calculated for Ls P2Ox
^bdata taken from reference [9]
Kinetic data were determined at 30°C, pH 6.5 and using D-glucose (100 mM) as saturating electron donor.

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ISSN: 1475-2859

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