Microbial Cell Factories

Table 1 Kinetics of wild-type (WT) and V108A l -iLDH

From: Rationally re-designed mutation of NAD-independent l-lactate dehydrogenase: high optical resolution of racemic mandelic acid by the engineered Escherichia coli

Substrate	WTl-iLDH			V108Al-iLDH
	K_cat(s^-1)	K_m(mM)	K_cat/K_m(mM^-1s^-1)	K_cat(s^-1)	K_m(mM)	K_cat/K_m(mM^-1s^-1)
l-Lactate	445 ± 44	0.18 ± 0.01	2472	185 ± 36	0.8 ± 0.1	231
l-Mandelate	8.3 ± 1.3	6.8 ± 1.0	1.2	97 ± 13	1.6 ± 0.1	61

All experiments were carried out at 30°C in 1 mL of 50 mM Tris–HCl (pH 7.5), with DCIP (0.0625 mM) as the electron acceptor. Values for k_cat are expressed as electrons transferred per second per molecule of enzyme. K_m values are expressed in terms of mM of substrate.

Back to article page

ISSN: 1475-2859

Contact us

Submission enquiries: journalsubmissions@springernature.com