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Literature summary for 1.18.1.2 extracted from

  • Catalano-Dupuy, D.L.; Musumeci, M.A.; Lopez-Rivero, A.; Ceccarelli, E.A.
    A highly stable plastidic-type ferredoxin-NADP(H) reductase in the pathogenic bacterium Leptospira interrogans (2011), PLoS ONE, 6, e26736.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.18.1.2

General Stability

General Stability Organism
persistence of a native folded structure is detected in up to 6 M urea, with 38% residual activity, the high stability might be due to robust interactions between the FAD and the NADP+ domains of the protein Leptospira interrogans

Organism

Organism UniProt Comment Textmining
Leptospira interrogans Q8EY89
-
-
Leptospira interrogans 56601 Q8EY89
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 reduced ferredoxin + NADP+ source of ferredoxin: Leptospira LB107 Leptospira interrogans 2 oxidized ferredoxin + NADPH + H+
-
 ?
2 reduced ferredoxin + NADP+ source of ferredoxin: Leptospira LB107 Leptospira interrogans 56601 2 oxidized ferredoxin + NADPH + H+
-
 ?
additional information enzyme additionally displays high diaphorase activity using artificial acceptors and functions as a ferric reductase Leptospira interrogans ?
-
 ?
additional information enzyme additionally displays high diaphorase activity using artificial acceptors and functions as a ferric reductase Leptospira interrogans 56601 ?
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
68.1
-
 melting temperature Leptospira interrogans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
-
 Leptospira interrogans

Cofactor

Cofactor Comment Organism Structure
FAD the high stability of the enzyme might be due to robust interactions between the FAD and the NADP+ domains of the protein Leptospira interrogans
NADPH
-
 Leptospira interrogans