The enzyme participates in the biosynthesis of several deoxysugars, including beta-L-4-epi-vancosamine, alpha-L-megosamine, L- and D-olivose, D-oliose, D-mycarose, forosamine and beta-L-digitoxose. In vitro the intermediate can undergo a spontaneous decomposition to maltol [2,3].
in forosamine biosynthesis, enzymes SpnO and SpnN function as a 2,3-dehydrase and a 3-ketoreductase, respectively. The two enzymes act sequentially to catalyze C-2 deoxygenation of TDP-4-dehydro-6-deoxy-D-glucose to form the SpnQ substrate, TDP-4-dehydro-2,6-dideoxy-D-glucose
the mtm-v gene encodes for a 2,3-dehydratase that catalyzes early and common steps in the biosyntheiss of the mithramycin sugars D-olivose, D-oliose and D-mycarose. Its inactivation causes the accumulation of the nonglycosylated intermediate premithramycinone
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to 1.7 A resolution. Each subunit of the EvaA dimer folds into two domains that clearly arose via gene duplication. Two dTDP-sugar binding pockets, A and B, are present in each EvaA subunit. Pocket A functions as the active site and pocket B is simply a remnant left behind from the gene duplication event
construction of a Streptomyces albus strain harboring the oleG2 glycosyltransferase gene and transformation with plasmid constructs containing a set of genes proposed to be required for the biosynthesis of dTDP-L-olivose and dTDP-L-oleandrose, respectively. Incubation of these strains with the erythromycin aglycon (erythronolide B) gives rise to two new glycosylated compounds, identified as L-3-O-olivosyl- and L-3-O-oleandrosyl-erythronolide B. Plasmid constructs pOLV and pOLE containing the oleW, oleV, oleL, oleS, oleE, and oleU genes and the 5' end of oleNI encode all enzyme activities required for the biosynthesis of these two 2,6-dideoxysugars