Reaction: D-ribitol 5-phosphate + NADP+ = D-ribulose 5-phosphate + NADPH + H+
Other name(s): acs1 (gene name); bcs1 (gene name); tarJ (gene name); ribulose-5-phosphate reductase; ribulose-5-P reductase; D-ribulose 5-phosphate reductase
Systematic name: D-ribitol-5-phosphate:NADP+ 2-oxidoreductase
Comments: 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Zolli, M., Kobric, D.J. and Brown, E.D. Reduction precedes cytidylyl transfer without substrate channeling in distinct active sites of the bifunctional CDP-ribitol synthase from Haemophilus influenzae. Biochemistry 40 (2001) 5041-5048. [PMID: 11305920]
2. Pereira, M.P. and Brown, E.D. Bifunctional catalysis by CDP-ribitol synthase: convergent recruitment of reductase and cytidylyltransferase activities in Haemophilus influenzae and Staphylococcus aureus. Biochemistry 43 (2004) 11802-11812. [PMID: 15362865]
3. Pereira, M.P., D'Elia, M.A., Troczynska, J. and Brown, E.D. Duplication of teichoic acid biosynthetic genes in Staphylococcus aureus leads to functionally redundant poly(ribitol phosphate) polymerases. J. Bacteriol. 190 (2008) 5642-5649. [PMID: 18556787]
4. Baur, S., Marles-Wright, J., Buckenmaier, S., Lewis, R.J. and Vollmer, W. Synthesis of CDP-activated ribitol for teichoic acid precursors in Streptococcus pneumoniae. J. Bacteriol. 191 (2009) 1200-1210. [PMID: 19074383]