EC 1.19.1.1 - Flavodoxin—NADP+ reductase

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IntEnz Enzyme Nomenclature
EC 1.19.1.1

Names

Accepted name:
flavodoxin—NADP+ reductase
Other name:
FPR
Systematic name:
flavodoxin:NADP+ oxidoreductase

Reaction

Cofactor

Comments:

A flavoprotein (FAD). This activity occurs in some prokaryotes and algae that possess flavodoxin, and provides low-potential electrons for a variety of reactions such as nitrogen fixation, sulfur assimilation and amino acid biosynthesis. In photosynthetic organisms it is involved in the photosynthetic electron transport chain. The enzyme also catalyses EC 1.18.1.2, ferredoxin—NADP+ reductase.

This activity occurs in some prokaryotes and algae that possess flavodoxin, and provides low-potential electrons for a variety of reactions such as nitrogen fixation, sulfur assimilation and amino acid biosynthesis. In photosynthetic organisms it is involved in the photosynthetic electron transport chain. The enzyme also catalyses EC 1.18.1.2.

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. McIver, L., Leadbeater, C., Campopiano, D. J., Baxter, R. L., Daff, S. N., Chapman, S. K., Munro, A. W.
    Characterisation of flavodoxin NADP+ oxidoreductase and flavodoxin; key components of electron transfer in Escherichia coli.
    Eur. J. Biochem. 257: 577-585 (1998). [PMID: 9839946]
  2. Leadbeater, C., McIver, L., Campopiano, D. J., Webster, S. P., Baxter, R. L., Kelly, S. M., Price, N. C., Lysek, D. A., Noble, M. A., Chapman, S. K., Munro, A. W.
    Probing the NADPH-binding site of Escherichia coli flavodoxin oxidoreductase.
    Biochem. J. 352 Pt 2: 257-266 (2000). [PMID: 11085917]
  3. Wan, J. T., Jarrett, J. T.
    Electron acceptor specificity of ferredoxin (flavodoxin):NADP+ oxidoreductase from Escherichia coli.
    Arch. Biochem. Biophys. 406: 116-126 (2002). [PMID: 12234497]
  4. Bortolotti, A., Perez-Dorado, I., Goni, G., Medina, M., Hermoso, J. A., Carrillo, N., Cortez, N.
    Coenzyme binding and hydride transfer in Rhodobacter capsulatus ferredoxin/flavodoxin NADP(H) oxidoreductase.
    Biochim. Biophys. Acta 1794: 199-210 (2009). [PMID: 18973834]
  5. Bortolotti, A., Sanchez-Azqueta, A., Maya, C. M., Velazquez-Campoy, A., Hermoso, J. A., Medina, M., Cortez, N.
    The C-terminal extension of bacterial flavodoxin-reductases: involvement in the hydride transfer mechanism from the coenzyme.
    Biochim. Biophys. Acta 1837: 33-43 (2014). [PMID: 24016470]
  6. Skråmo, S., Hersleth, H. P., Hammerstad, M., Andersson, K. K., Røhr, Å. K.
    Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of a ferredoxin/flavodoxin-NADP(H) oxidoreductase (Bc0385) from Bacillus cereus.
    Acta Crystallogr F Struct Biol Commun 70: 777-780 (2014). [PMID: 24915092]

[EC 1.19.1.1 created 2016]