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Literature summary extracted from

  • Aliverti, A.; Pandini, V.; Zanetti, G.
    Domain exchange between isoforms of ferredoxin-NADP+ reductase produces a functional enzyme (2004), Biochim. Biophys. Acta, 1696, 93-101.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.18.1.2 functional expression of chimeric enzyme, comprising the root NADP-binding domain and the leaf FAD-binding domain, in Escherichia coli Spinacia oleracea

Protein Variants

EC Number Protein Variants Comment Organism
1.18.1.2 additional information construction of 2 different chimeric enzymes with domains of spinach nonphotosynthetic root isozyme and photosynthetic leaf isozyme, the chimera comprising the root NADP-binding domain and the leaf FAD-binding domain is functional, while the chimera with opposite composition is not, the active chimera shows partially impaired intermolecular electron transfer, and highly increased NADPH-diaphorase activity, and increased activity with NADH as cofactor compared to the parent isozymes, improvement of catalytic properties, overview Spinacia oleracea

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.18.1.2 additional information
-
 additional information steady-state kinetics and dissociation constants of NADPH-enzyme complex, wild-type isozymes and recombinant chimera Spinacia oleracea
1.18.1.2 0.0025
-
 reduced ferredoxin I pH 7.0, 15°C, wild-type root isozyme Spinacia oleracea
1.18.1.2 0.0026
-
 reduced ferredoxin I pH 7.0, 15°C, wild-type leaf isozyme Spinacia oleracea
1.18.1.2 0.0027
-
 reduced ferredoxin I pH 7.0, 15°C, recombinant chimeric enzyme Spinacia oleracea
1.18.1.2 0.0074
-
 NADPH pH 7.0, 15°C, recombinant chimeric enzyme, diaphorase activity Spinacia oleracea
1.18.1.2 0.012
-
 NADPH pH 7.0, 15°C, wild-type root isozyme, diaphorase activity Spinacia oleracea
1.18.1.2 0.035
-
 NADPH pH 7.0, 15°C, wild-type leaf isozyme, diaphorase activity Spinacia oleracea
1.18.1.2 4.2
-
 NADH pH 7.0, 15°C, recombinant chimeric enzyme Spinacia oleracea

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.18.1.2 reduced ferredoxin + NADP+ Spinacia oleracea
-
 oxidized ferredoxin + NADPH
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.18.1.2 Spinacia oleracea
-
 2 tissue-specific isozymes in leaf and root
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.18.1.2 recombinant chimeric enzyme, comprising the root NADP-binding domain and the leaf FAD-binding domain, from Escherichia coli Spinacia oleracea

Reaction

EC Number Reaction Comment Organism Reaction ID
1.18.1.2 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH ping pong bi bi mechanism Spinacia oleracea
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.18.1.2 leaf photosynthetic leaf isozyme Spinacia oleracea
-
1.18.1.2 root nonphotosynthetic root isozyme Spinacia oleracea
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.18.1.2 additional information
-
-
 Spinacia oleracea

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.1.2 2 ferricyanide + NAD(P)H diaphorase activity Spinacia oleracea 2 ferrocyanide + NAD(P)+ + H+
-
 ?
1.18.1.2 additional information structure-function analysis of isozymes and chimeric mutant thereof Spinacia oleracea ?
-
 ?
1.18.1.2 oxidized ferredoxin I + NADH + H+
-
 Spinacia oleracea reduced ferredoxin I + NAD+
-
 ?
1.18.1.2 reduced ferredoxin + NADP+
-
 Spinacia oleracea oxidized ferredoxin + NADPH
-
 ?
1.18.1.2 reduced ferredoxin I + NADP+
-
 Spinacia oleracea oxidized ferredoxin I + NADPH
-
 r
1.18.1.2 reduced ferredoxin I + NADP+
-
 Spinacia oleracea oxidized ferredoxin I + NADPH + H+
-
 r

Synonyms

EC Number Synonyms Comment Organism
1.18.1.2 FNR
-
 Spinacia oleracea

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.18.1.2 additional information
-
 enzyme thermal inactivation is irreversible Spinacia oleracea
1.18.1.2 15
-
 assay at Spinacia oleracea

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.18.1.2 55
-
 recombinant chimeric enzyme is slightly less stable than the wild-type parent isozymes Spinacia oleracea

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.18.1.2 9.6
-
 NADH pH 7.0, 15°C, recombinant chimeric enzyme, diaphorase activity Spinacia oleracea
1.18.1.2 45
-
 reduced ferredoxin I pH 7.0, 15°C, recombinant chimeric enzyme Spinacia oleracea
1.18.1.2 82
-
 reduced ferredoxin I pH 7.0, 15°C, wild-type leaf isozyme Spinacia oleracea
1.18.1.2 115
-
 reduced ferredoxin I pH 7.0, 15°C, wild-type root isozyme Spinacia oleracea
1.18.1.2 500
-
 NADPH pH 7.0, 15°C, wild-type leaf isozyme, diaphorase activity Spinacia oleracea
1.18.1.2 520
-
 NADPH pH 7.0, 15°C, wild-type root isozyme, diaphorase activity Spinacia oleracea
1.18.1.2 560
-
 NADPH pH 7.0, 15°C, recombinant chimeric enzyme, diaphorase activity Spinacia oleracea

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.18.1.2 7
-
 assay at Spinacia oleracea

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.1.2 FAD
-
 Spinacia oleracea
1.18.1.2 NAD(P)H NADPH is absolutely preferred over NADH by the wild-type isozymes Spinacia oleracea
1.18.1.2 NADP+
-
 Spinacia oleracea