• BMB Reports
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• v.32 no.1
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• pp.72-75
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• 1999

In an effort to understand the function of the eryBVII gene in the erythromycin biosynthetic gene cluster, we overexpressed the eryBVII gene in E. coli and TDP-6-deoxy-L-threo-D-glycero-4-hexulose was used as a substrate of the overexpressed EryBVII enzyme. The enzymatic reaction product was chemically modified by reduction and peracetylation. Structural analysis of the derivatized enzymatic products by GC-Mass Spectrophotometry indicated that TDP-6-deoxy-L-threo-D-glycero-4-hexulose could be converted into its epimer by EryBVII enzyme. Based on this result, TDP-6-deoxy-L-threo-D-glycero-4-hexulose was indeed the substrate of EryBVII enzyme and the function of the eryBVII gene was confirmed.