当前位置:首页 >> 生物学 >>

NADH-cofactor specificity of the highly active AdhZ3and AdhZ2 from Escherichia coli K-12


Improving the NADH-cofactor specificity of The highly active AdhZ3and AdhZ2 from Escherichia coli K-12
Biocatalysis is a promising tool for the production of chemicals. But when cofactor depending enzymatic reactions are involved, the applicability of the right cofactor is a central issue. In this paper, the researchers reported the production of alcohol by nicotinamide cofactor (NAD (P) +) depending alcohol dehydrogenases. AdhZ3 and AdhZ2 from E.coli, has a preference for NADPH as cofactor, which are important for the production of alcohols from biomass. In this paper, the workers used site-saturation mutagenesis, enzyme expression and purification; Enzyme assays, determination of kinetic parameters, protein comparison and structure modeling to construct a rational experiment, to improve the NADH-cofactor specificity. In my opinion, innovative points is (1) the structure guided site-specific random approach can change the cofactor preference towards NADH, and can deduce more general rules for redesigning the cofactor specificity. (2) A combinatorial site saturation mutagenesis altering three residues was applied. In conclusion, this literature showed that improving the NADH-cofactor specificity of the highly active AdhZ3 and AdhZ2 can increase the production of alcohols from biomass.


相关文章: