| EC |
1.1.1.405 |
| Accepted name: |
ribitol-5-phosphate 2-dehydrogenase (NADP+) |
| 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 |
| 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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 19074383] |
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| [EC 1.1.1.405 created 2017] |
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