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Literature summary for 1.18.1.2 extracted from

  • Ceccarelli, E.A.; Arakaki, A.K.; Cortez, N.; Carrillo, N.
    Functional plasticity and catalytic efficiency in plant and bacterial ferredoxin-NADP(H) reductases (2004), Biochim. Biophys. Acta, 1698, 155-165.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information forward and reverse reactions follow different kinetic mechanism, overview Cyanophora paradoxa
additional information
-
additional information forward and reverse reactions follow different kinetic mechanism, overview Chlamydomonas reinhardtii
additional information
-
additional information forward and reverse reactions follow different kinetic mechanism, overview Escherichia coli
additional information
-
additional information forward and reverse reactions follow different kinetic mechanism, overview Spinacia oleracea
additional information
-
additional information forward and reverse reactions follow different kinetic mechanism, overview Rhodobacter capsulatus
additional information
-
additional information forward and reverse reactions follow different kinetic mechanism, overview Azotobacter vinelandii
additional information
-
additional information forward and reverse reactions follow different kinetic mechanism, overview Anabaena sp.
additional information
-
additional information forward and reverse reactions follow different kinetic mechanism, overview Leptospira interrogans

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
Spinacia oleracea 9507
-
additional information nucleus-encoded enzyme Cyanophora paradoxa
-
-
plastid
-
Spinacia oleracea 9536
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli enzyme is involved in anaerobic metabolism, phylogenetic evolution, relationships, and classification, overview ?
-
?
additional information Azotobacter vinelandii enzyme is involved in nitrogenase reduction, phylogenetic evolution, relationships, and classification, overview ?
-
?
additional information Spinacia oleracea enzyme is involved in photosynthesis and nitrite assimilation, phylogenetic evolution, relatiionships, and classification, overview ?
-
?
additional information Chlamydomonas reinhardtii phylogenetic evolution, relatiionships, and classification, overview ?
-
?
additional information Rhodobacter capsulatus phylogenetic evolution, relatiionships, and classification, overview ?
-
?
additional information Leptospira interrogans phylogenetic evolution, relatiionships, and classification, overview ?
-
?
additional information Cyanophora paradoxa phylogenetic evolution, relationships, and classification, overview ?
-
?
additional information Anabaena sp. phylogenetic evolution, relationships, and classification, overview ?
-
?
additional information Anabaena sp. PCC7119 phylogenetic evolution, relationships, and classification, overview ?
-
?
reduced ferredoxin + NADP+ Cyanophora paradoxa
-
oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+ Chlamydomonas reinhardtii
-
oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+ Escherichia coli
-
oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+ Spinacia oleracea
-
oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+ Rhodobacter capsulatus
-
oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+ Azotobacter vinelandii
-
oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+ Anabaena sp.
-
oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+ Leptospira interrogans
-
oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+ Anabaena sp. PCC7119
-
oxidized ferredoxin + NADPH
-
r

Organism

Organism UniProt Comment Textmining
Anabaena sp.
-
PCC7119
-
Anabaena sp. PCC7119
-
PCC7119
-
Azotobacter vinelandii
-
-
-
Chlamydomonas reinhardtii
-
-
-
Cyanophora paradoxa
-
-
-
Escherichia coli
-
-
-
Leptospira interrogans
-
parasitic bacterium
-
Rhodobacter capsulatus
-
-
-
Spinacia oleracea
-
-
-

Reaction

Reaction Comment Organism Reaction ID
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH catalytic mechanism of forward and reverse reactions Cyanophora paradoxa
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH catalytic mechanism of forward and reverse reactions Chlamydomonas reinhardtii
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH catalytic mechanism of forward and reverse reactions Escherichia coli
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH catalytic mechanism of forward and reverse reactions Spinacia oleracea
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH catalytic mechanism of forward and reverse reactions Rhodobacter capsulatus
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH catalytic mechanism of forward and reverse reactions Azotobacter vinelandii
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH catalytic mechanism of forward and reverse reactions Anabaena sp.
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH catalytic mechanism of forward and reverse reactions Leptospira interrogans

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Spinacia oleracea
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme is involved in anaerobic metabolism, phylogenetic evolution, relationships, and classification, overview Escherichia coli ?
-
?
additional information enzyme is involved in nitrogenase reduction, phylogenetic evolution, relationships, and classification, overview Azotobacter vinelandii ?
-
?
additional information enzyme is involved in photosynthesis and nitrite assimilation, phylogenetic evolution, relatiionships, and classification, overview Spinacia oleracea ?
-
?
additional information phylogenetic evolution, relatiionships, and classification, overview Chlamydomonas reinhardtii ?
-
?
additional information phylogenetic evolution, relatiionships, and classification, overview Rhodobacter capsulatus ?
-
?
additional information phylogenetic evolution, relatiionships, and classification, overview Leptospira interrogans ?
-
?
additional information phylogenetic evolution, relationships, and classification, overview Cyanophora paradoxa ?
-
?
additional information phylogenetic evolution, relationships, and classification, overview Anabaena sp. ?
-
?
additional information phylogenetic evolution, relationships, and classification, overview Anabaena sp. PCC7119 ?
-
?
NADPH + acceptor diaphorase activity, acceptors can be complexed metals or aromatic molecules Anabaena sp. NADP+ + reduced acceptor
-
?
NADPH + acceptor diaphorase activity, acceptors can be complexed metals or aromatic molecules Anabaena sp. PCC7119 NADP+ + reduced acceptor
-
?
reduced ferredoxin + NADP+
-
Cyanophora paradoxa oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+
-
Chlamydomonas reinhardtii oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+
-
Escherichia coli oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+
-
Spinacia oleracea oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+
-
Rhodobacter capsulatus oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+
-
Azotobacter vinelandii oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+
-
Anabaena sp. oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+
-
Leptospira interrogans oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+ association of ferredoxin with the enzyme is steered by electrostatic interactions Cyanophora paradoxa oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+ association of ferredoxin with the enzyme is steered by electrostatic interactions Chlamydomonas reinhardtii oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+ association of ferredoxin with the enzyme is steered by electrostatic interactions Escherichia coli oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+ association of ferredoxin with the enzyme is steered by electrostatic interactions Rhodobacter capsulatus oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+ association of ferredoxin with the enzyme is steered by electrostatic interactions Azotobacter vinelandii oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+ association of ferredoxin with the enzyme is steered by electrostatic interactions Anabaena sp. oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+ association of ferredoxin with the enzyme is steered by electrostatic interactions Leptospira interrogans oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+ ferredoxin contains a [2Fe2S] cluster and binds to the concave surface of the FAD domain, association of ferredoxin with the enzyme is steered by electrostatic interactions Spinacia oleracea oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+
-
Anabaena sp. PCC7119 oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+ association of ferredoxin with the enzyme is steered by electrostatic interactions Anabaena sp. PCC7119 oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+
-
Chlamydomonas reinhardtii oxidized ferredoxin + NADPH + H+
-
r
reduced ferredoxin + NADP+
-
Escherichia coli oxidized ferredoxin + NADPH + H+
-
r
reduced ferredoxin + NADP+
-
Spinacia oleracea oxidized ferredoxin + NADPH + H+
-
r
reduced ferredoxin + NADP+
-
Azotobacter vinelandii oxidized ferredoxin + NADPH + H+
-
r
reduced ferredoxin + NADP+
-
Anabaena sp. oxidized ferredoxin + NADPH + H+
-
r
reduced ferredoxin + NADP+
-
Anabaena sp. PCC7119 oxidized ferredoxin + NADPH + H+
-
r
reduced flavodoxin + NADP+
-
Escherichia coli oxidized flavodoxin + NADPH + H+
-
r

Subunits

Subunits Comment Organism
More 2-domain structure Cyanophora paradoxa
More 2-domain structure Chlamydomonas reinhardtii
More 2-domain structure Rhodobacter capsulatus
More 2-domain structure Leptospira interrogans
More 2-domain structure, structure analysis Escherichia coli
More 2-domain structure, structure analysis Spinacia oleracea
More 2-domain structure, structure analysis Azotobacter vinelandii
More 2-domain structure, structure analysis Anabaena sp.

Synonyms

Synonyms Comment Organism
ferredoxin (flavodoxin)-NADP(H) reductase
-
Cyanophora paradoxa
ferredoxin (flavodoxin)-NADP(H) reductase
-
Chlamydomonas reinhardtii
ferredoxin (flavodoxin)-NADP(H) reductase
-
Escherichia coli
ferredoxin (flavodoxin)-NADP(H) reductase
-
Spinacia oleracea
ferredoxin (flavodoxin)-NADP(H) reductase
-
Rhodobacter capsulatus
ferredoxin (flavodoxin)-NADP(H) reductase
-
Azotobacter vinelandii
ferredoxin (flavodoxin)-NADP(H) reductase
-
Anabaena sp.
ferredoxin (flavodoxin)-NADP(H) reductase
-
Leptospira interrogans
ferredoxin-NADP(H) reductase
-
Cyanophora paradoxa
ferredoxin-NADP(H) reductase
-
Chlamydomonas reinhardtii
ferredoxin-NADP(H) reductase
-
Escherichia coli
ferredoxin-NADP(H) reductase
-
Spinacia oleracea
ferredoxin-NADP(H) reductase
-
Rhodobacter capsulatus
ferredoxin-NADP(H) reductase
-
Azotobacter vinelandii
ferredoxin-NADP(H) reductase
-
Anabaena sp.
ferredoxin-NADP(H) reductase
-
Leptospira interrogans
FNR
-
Cyanophora paradoxa
FNR
-
Chlamydomonas reinhardtii
FNR
-
Escherichia coli
FNR
-
Spinacia oleracea
FNR
-
Rhodobacter capsulatus
FNR
-
Azotobacter vinelandii
FNR
-
Anabaena sp.
FNR
-
Leptospira interrogans
More enzyme belongs more to the plant-type enzyme family than to the bacterial-type enzyme family Cyanophora paradoxa
More enzyme belongs to the bacterial-type enzyme family Escherichia coli
More enzyme belongs to the bacterial-type enzyme family Azotobacter vinelandii
More enzyme belongs to the plant-type enzyme family Chlamydomonas reinhardtii
More enzyme belongs to the plant-type enzyme family Spinacia oleracea
More enzyme belongs to the plant-type enzyme family Rhodobacter capsulatus
More enzyme belongs to the plant-type enzyme family Anabaena sp.
More enzyme belongs to the plant-type enzyme family, result of lateral gene transfer Leptospira interrogans

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information low efficiency Rhodobacter capsulatus
additional information
-
additional information low efficiency Azotobacter vinelandii
additional information
-
additional information the low efficiency is intrinsic to the reductase itself Escherichia coli
0.004
-
reduced flavodoxin flavodoxin I or II Escherichia coli
0.15
-
reduced ferredoxin
-
Escherichia coli
1
-
reduced ferredoxin
-
Azotobacter vinelandii
90 174 reduced ferredoxin
-
Chlamydomonas reinhardtii
200 600 reduced ferredoxin
-
Spinacia oleracea
200 600 reduced ferredoxin
-
Anabaena sp.

Cofactor

Cofactor Comment Organism Structure
FAD extended conformation Cyanophora paradoxa
FAD extended conformation Chlamydomonas reinhardtii
FAD extended conformation Rhodobacter capsulatus
FAD extended conformation Leptospira interrogans
FAD extended conformation, interaction via Tyr96, direct electron transfer between FAD and ferredoxin [2Fe2S] center, modeling of conformation of C4alpha polypeptide backbone and FAD Spinacia oleracea
FAD extended conformation, modeling of conformation of C4alpha polypeptide backbone and FAD, binding domain is N-terminal Anabaena sp.
FAD folded conformation, modeling of conformation of C4alpha polypeptide backbone and FAD, binding domain is N-terminal Escherichia coli
FAD folded conformation, modeling of conformation of C4alpha polypeptide backbone and FAD, binding domain is N-terminal Azotobacter vinelandii
additional information poor activity with NAD(H) Anabaena sp.
NADP+
-
Cyanophora paradoxa
NADP+
-
Chlamydomonas reinhardtii
NADP+
-
Rhodobacter capsulatus
NADP+
-
Leptospira interrogans
NADP+ C-terminal binding domain Escherichia coli
NADP+ C-terminal binding domain Azotobacter vinelandii
NADP+ C-terminal binding domain Anabaena sp.
NADP+ interaction via Tyr314, binding site at the C-terminus Spinacia oleracea
NADPH
-
Cyanophora paradoxa
NADPH
-
Chlamydomonas reinhardtii
NADPH
-
Rhodobacter capsulatus
NADPH
-
Leptospira interrogans
NADPH C-terminal binding domain Escherichia coli
NADPH C-terminal binding domain Azotobacter vinelandii
NADPH C-terminal binding domain Anabaena sp.
NADPH interaction via Tyr314, binding site at the C-terminus Spinacia oleracea