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

BRENDA support

Literature summary extracted from

  • Wang, A.; Zeng, Y.; Han, H.; Weeratunga, S.; Morgan, B.N.; Moenne-Loccoz, P.; Schoenbrunn, E.; Rivera, M.
    Biochemical and structural characterization of Pseudomonas aeruginosa Bfd and FPR: ferredoxin NADP+ reductase and not ferredoxin is the redox partner of heme oxygenase under iron-starvation conditions (2007), Biochemistry, 46, 12198-12211.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.18.1.2 expressed in Escherichia coli ArcticExpress RIL cells Pseudomonas aeruginosa

Organism

EC Number Organism UniProt Comment Textmining
1.18.1.2 Pseudomonas aeruginosa
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.18.1.2 Q-Sepharose Fast Flow column chromatography and Sephadex G-50 gel filtration Pseudomonas aeruginosa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.1.2 additional information FPR supports the efficient degradation of heme by heme oxygenase Pseudomonas aeruginosa ?
-
 ?
1.18.1.2 oxidized ferredoxin + NADH very slow and inefficient reaction Pseudomonas aeruginosa reduced ferredoxin + NAD+
-
 ?
1.18.1.2 reduced ferredoxin + NADP+ NADPH is the reducing agent of FPR in vivo Pseudomonas aeruginosa oxidized ferredoxin + NADPH
-
 r

Synonyms

EC Number Synonyms Comment Organism
1.18.1.2 ferredoxin NADP+ reductase
-
 Pseudomonas aeruginosa
1.18.1.2 FPR
-
 Pseudomonas aeruginosa
1.18.1.2 NADPH-dependent ferredoxin reductase
-
 Pseudomonas aeruginosa

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.1.2 FAD FAD is reduced rapidly and completely when the enzyme reacts with NADPH, while in contrast, addition of NADH results in very slow and inefficient reduction Pseudomonas aeruginosa
1.18.1.2 NADP+
-
 Pseudomonas aeruginosa