EC 1.1.1.405 - Ribitol-5-phosphate 2-dehydrogenase (NADP+)

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IntEnz Enzyme Nomenclature
EC 1.1.1.405

Names

Accepted name:
ribitol-5-phosphate 2-dehydrogenase (NADP+)
Other names:
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

Reaction

Cofactor

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Zolli, M., Kobric, D. J., 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 : 5041-5048 (2001). [PMID: 11305920]
  2. Pereira, M. P., Brown, E. D.
    Bifunctional catalysis by CDP-ribitol synthase: convergent recruitment of reductase and cytidylyltransferase activities in Haemophilus influenzae and Staphylococcus aureus.
    Biochemistry 43 : 11802-11812 (2004). [PMID: 15362865]
  3. Pereira, M. P., D'Elia, M. A., Troczynska, J., Brown, E. D.
    Duplication of teichoic acid biosynthetic genes in Staphylococcus aureus leads to functionally redundant poly(ribitol phosphate) polymerases.
    J. Bacteriol. 190 : 5642-5649 (2008). [PMID: 18556787]
  4. Baur, S., Marles-Wright, J., Buckenmaier, S., Lewis, R. J., Vollmer, W.
    Synthesis of CDP-activated ribitol for teichoic acid precursors in Streptococcus pneumoniae.
    J. Bacteriol. 191 : 1200-1210 (2009). [PMID: 19074383]

[EC 1.1.1.405 created 2017]