Two series of innovative 2′-deoxy nucleoside analogues have been designed where the nucleobase has been split into its imidazole and pyrimidine subunits. This structural modification serves to introduce flexibility into the nucleobase scaffold while still retaining the elements required for recognition. The synthetic efforts to realize these analogues are described within.
This paper describes the adaptation of a simple colorimetric assay for inorganic pyrophosphate to the enzyme 3-deoxy-d-manno-octulosonate cytidylyltransferase(CMP-KDO synthetase, KdsB, E.C. 2.7.7.38), a key enzyme in the biosynthesis of lipopolysaccharide (LPS) in Gram-negative organisms. This assay is particularly useful because it can be combined with the malachite green assay for inorganic phosphateto form an assay system capable of determining inorganic phosphate and inorganic pyrophosphate in the same solution (the MG/EK assay). This assay system has the potential for simultaneous screening of the 3-deoxy-d-manno-octulosonate (KDO) biosynthesis pathway. We test this potential using two enzymes, KdsB and KdsC, involved in the biosynthesis and utilization of the key bacterial 8-carbon sugar, KDO.
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