Arabinose 5-phosphate 2-deoxy-2-fluoro

Deoxy-3-fluoro-D-glucose (see Section 11,2), a weak substrate for yeast hexokinase, is phosphorylated enzymically - to give the 6-phosphate 588, which is transformed into 2-deoxy-2-fluoro-D-arabinose 5-phos-phate (589) by lead tetraacetate oxidation. 

The requirement of the remaining enzymes, KD0-8-phosphate synthase, KD0-8-phosphate phosphatase and CMP-KDO synthetase, for their natural substrates, D-arabinose-5-phosphate + PEP, KD0-8-phosphate and KDO + CTP, respectively, was specific and the inhibition studies with substrate analogues were disappointing. Of the compounds tested as potential substrates of KD0-8-phosphate synthase, only the isosteric phosphonate analogue (Compound 11, Table III) of D-arabinose-5-phosphate was an alternate substrate (see Ref. 28). There were a number of weak competitive inhibitors of the synthase reaction (Compounds 2, 5, 6, 7, 15,and 19,Table III) the best inhibitor of the synthase reaction was 2-deoxy-2-fluoro-D-arabinonate-5-phosphate (compound 14, Table III). 

Oligonucleotides containing 2 -deoxy-2 -fluoro-D-arabinose or -D-ribose form stable, triple-heUcal complexes stabilized by the intermolecular 2 -OH phosphate contacts and sugar puckering these derivatives have promoted interest in relation to compounds synthesized for DNA targeting in vivo Fig. 6 [31]. 

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