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

BRENDA support

Literature summary for 1.18.1.2 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)

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

Protein Variants

Protein Variants Comment Organism
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]

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Purification (Commentary)

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

Reaction

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

Source Tissue

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
FNR
-
Spinacia oleracea

Temperature Optimum [°C]

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

Temperature Stability [°C]

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

Turnover Number [1/s]

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

pH Optimum

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

Cofactor

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