Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Hermoso, J.A.; Mayoral, T.; Faro, M.; Gomez-Moreno, C.; Sanz-Aparicio, J.; Medina, M.
    Mechanism of coenzyme recognition and binding revealed by crystal structure analysis of ferredoxin-NADP+ reductase complexed with NADP+ (2002), J. Mol. Biol., 319, 1133-1142.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.18.1.2 enzyme complexed with NADP+, X-ray diffraction structure determination and analysis at 2.1 A resolution Anabaena sp.

Organism

EC Number Organism UniProt Comment Textmining
1.18.1.2 Anabaena sp.
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.18.1.2 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH mechanism of coenzyme recognition and binding Anabaena sp.
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.1.2 reduced ferredoxin + NADP+ hydride transfer between FAD and NADP+, highly specific for NADP+ versus NAD+, mechnanism Anabaena sp. oxidized ferredoxin + NADPH
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.18.1.2 FNR
-
 Anabaena sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.1.2 FAD prosthetic group, flavoenzyme Anabaena sp.
1.18.1.2 NADP+ binding structure, binding causes conformational changes in the enzyme and creation of a new binding pocket near the FAD binding site Anabaena sp.