Requires Zn2+. The enzyme, characterized in bacteria, is specific for NADP. It is part of the synthesis pathway of CDP-ribitol. In Haemophilus influenzae it is part of a multifunctional enzyme also catalysing EC 2.7.7.40, D-ribitol-5-phosphate cytidylyltransferase. cf. EC 1.1.1.137, ribitol-5-phosphate 2-dehydrogenase.
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The enzyme appears in viruses and cellular organisms
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SYSTEMATIC NAME
IUBMB Comments
D-ribitol-5-phosphate:NADP+ 2-oxidoreductase
Requires Zn2+. The enzyme, characterized in bacteria, is specific for NADP. It is part of the synthesis pathway of CDP-ribitol. In Haemophilus influenzae it is part of a multifunctional enzyme also catalysing EC 2.7.7.40, D-ribitol-5-phosphate cytidylyltransferase. cf. EC 1.1.1.137, ribitol-5-phosphate 2-dehydrogenase.
the data suggest that NADPH binds first and ribulose 5-phosphate binds second. Bifunction enzyme catalyzing the reactions of EC 1.1.1.137 and EC 2.7.7.40, ordered bi-bi mechanism
tarI encodes an orthologue of the cytidylyltransferase domain of Bcs1 from Haemophilus influenzae and tarJ encodes an analogue of the reductase domain of Bcs1, TarI and TyrJ form a functional CDP-ribitol synthase complex. Release and free diffusion of the intermediate ribitol 5-phosphate without channelling between active sites, ordered bi-bi mechanism
the dehydrogenase activity of Acs1 is specific for ribulose 5-phosphate and NADPH in one direction and for ribitol 5-phosphate and NADP+ in the other direction. The activity is about twofold higher with ribulose 5-phosphate as the substrate than with ribose 5-phosphate. No substrate: xylulose 5-phosphate
the synthase first catalyzes the reduction of D-ribulose 5-phosphate followed by cytidylyl transfer to D-ribitol 5-phosphate, with a 650fold kinetic preference for cytidylyl transfer to D-ribitol 5-phosphate over D-ribulose 5-phosphate
Acs1 encodes a bifunctional enzyme that converts ribulose 5-phosphate into ribitol 5-phosphate and further into CDP-ribitol, the activated precursor form for incorporation of ribitol 5-phosphate into the Haemophilus influenzae type a capsular polysaccharide
2 * 26000 + 2 * 41000, tarI encodes an orthologue of the cytidylyltransferase domain of Bcs1 from Haemophilus influenzae and tarJ encodes an analogue of the reductase domain of Bcs1, TarI and TyrJ form a functional CDP-ribitol synthase complex, SDS-PAGE
2 * 26000 + 2 * 41000, tarI encodes an orthologue of the cytidylyltransferase domain of Bcs1 from Haemophilus influenzae and tarJ encodes an analogue of the reductase domain of Bcs1, TarI and TyrJ form a functional CDP-ribitol synthase complex, SDS-PAGE
2 * 26000 + 2 * 41000, tarI encodes an orthologue of the cytidylyltransferase domain of Bcs1 from Haemophilus influenzae and tarJ encodes an analogue of the reductase domain of Bcs1, TarI and TyrJ form a functional CDP-ribitol synthase complex, SDS-PAGE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
23°C, at 0.3 mg/ml in the presence of 20 mM HEPES, pH 7.1, 1 mM DTT, and 0.5 mg of BSA/ml, ribitol 5-phosphate dehydrogenase activity decreases to about 50% of the initial activity after 2 h
spr1148 gene amplified, inserted into plasmid pJFK118EH and transformed into competent cells of Escherichia coli DH5alpha. Plasmid pJFK118EH1148 isolated and insert with the spr1148 gene cut off by restriction enzymes NdeI and SacI. Fragment ligated into the overexpression plasmid pET28a(+) to generate plasmid pET1148. The plasmid transformed into Escherichia coli BL21(DE3) for overexpression of spr1148
Reduction precedes cytidylyl transfer without substrate channeling in distinct active sites of the bifunctional CDP-ribitol synthase from Haemophilus influenzae
Bifunctional catalysis by CDP-ribitol synthase: convergent recruitment of the reductase and cytidylyltransferase activities in Haemophilus influenzae and Staphylococcus aureus