1.18.1.2: ferredoxin-NADP+ reductase
This is an abbreviated version!
For detailed information about ferredoxin-NADP+ reductase, go to the full flat file.
Word Map on EC 1.18.1.2
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1.18.1.2
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nitrate
-
ferredoxins
-
denitrification
-
denitrify
-
reductases
-
heme
-
fad
-
spinach
-
chloroplast
-
copper
-
ammonia
-
nitrous
-
flavin
-
dissimilatory
-
photosystems
-
flavodoxins
-
denitrificans
-
alcaligenes
-
paracoccus
-
n2o
-
anabaena
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copper-containing
-
thylakoids
-
anammox
-
p450scc
-
semiquinone
-
diaphorase
-
viologen
-
azurins
-
ferredoxin-dependent
-
stutzeri
-
plant-type
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achromobacter
-
flavoenzymes
-
electron-transfer
-
ammonia-oxidizing
-
plastocyanin
-
dinitrogen
-
photoreduction
-
gogat
-
pregnenolone
-
nitrate-induced
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xylosoxidans
-
photoreduced
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wolinella
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isoalloxazine
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nitrate-reducing
-
biotechnology
-
nitrosomonas
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deoxyhemoglobin
-
agriculture
-
single-electron
- 1.18.1.2
- nitrate
- ferredoxins
-
denitrification
-
denitrify
- reductases
- heme
- fad
- spinach
- chloroplast
- copper
- ammonia
-
nitrous
- flavin
-
dissimilatory
- photosystems
- flavodoxins
- denitrificans
- alcaligenes
- paracoccus
- n2o
- anabaena
-
copper-containing
- thylakoids
-
anammox
- p450scc
- semiquinone
- diaphorase
- viologen
- azurins
-
ferredoxin-dependent
- stutzeri
-
plant-type
- achromobacter
-
flavoenzymes
-
electron-transfer
-
ammonia-oxidizing
- plastocyanin
-
dinitrogen
-
photoreduction
- gogat
- pregnenolone
-
nitrate-induced
- xylosoxidans
-
photoreduced
-
wolinella
- isoalloxazine
-
nitrate-reducing
- biotechnology
- nitrosomonas
-
deoxyhemoglobin
- agriculture
-
single-electron
Reaction
2 reduced ferredoxin
+
Synonyms
ABO_0145, adrenodoxin reductase, AnFNR, BsFNR, CT1512, cytochrome b6f -associated ferredoxin:NADP+ oxidoreductase, DA1, EC 1.6.7.1, EC 1.6.99.4, Fd-NADP+ reductase, ferredoxin (flavodoxin)-(reduced) nicotinamide adenine dinucleotide phosphate reductase, ferredoxin (flavodoxin)-NAD(P)H reductase, ferredoxin (flavodoxin)-NADP(H) reductase, ferredoxin (flavodoxin):NADP+ oxidoreductase, ferredoxin NADP oxidoreductase, ferredoxin NADP reductase, ferredoxin NADP(H) oxidoreductase, ferredoxin NADP+ oxidoreductase, ferredoxin NADP+ reductase, ferredoxin nicotinamide adenine dinucleotide phosphate reductase, ferredoxin-NAD(P)+ oxidoreductase, ferredoxin-NAD(P)+ reductase, ferredoxin-NAD(P)H reductase, ferredoxin-NADP oxidoreductase, ferredoxin-NADP reductase, Ferredoxin-NADP(+) reductase, ferredoxin-NADP(H) oxidoreductase, ferredoxin-NADP(H) reductase, ferredoxin-NADP+ oxidoreductase, ferredoxin-NADP+ reductase, ferredoxin-NADP+-oxidoreductase, ferredoxin-NADP+-reductase, ferredoxin-NADP-oxidoreductase, ferredoxin-NADP-reductase, ferredoxin-nicotinamide adenine dinucleotide phosphate reductase, ferredoxin-nicotinamide-adenine dinucleotide phosphate (oxidized) reductase, ferredoxin-TPN reductase, ferredoxin: NADP(+) oxidoreductase, ferredoxin: NADP+ oxidoreductase, ferredoxin:NADP oxidoreductase, ferredoxin:NADP(+) oxidoreductase, ferredoxin:NADP(H) oxidoreductase, ferredoxin:NADP(H) oxidoreductase 2, ferredoxin:NADP+ oxidoreductase, ferredoxin:NADP+ reductase, ferredoxin:NADPH oxidoreductase, ferric reductase, Flavodoxin reductase, FLDR, FLXR, FNR, FNR-A, FNR-B, FNR1, FNR2, FNRII, FNRL, FNRS, FPR, FprA, FprB, Fprs, LFNR1, LFNR2, mitochondrial-type ferredoxin:NADP+ reductase, More, mtFNR, NADH-dependent reduced ferredoxin:NADP oxidoreductase, NADP:ferredoxin oxidoreductase, NADPH ferredoxin reductase, NADPH-dependent ferredoxin reductase, NADPH:ferredoxin oxidoreductase, NfnAB, NfnIII, NFR, PETH, PfFNR, pFNR, photosynthetic ferredoxin NADP+ oxidoreductase, photosynthetic FNR, plastidic-type ferredoxin-NADP+ reductase, PP4_41290, RcFPR, reduced nicotinamide adenine dinucleotide phosphate-adrenodoxin reductase, reductase, ferredoxin-nicotinamide adenine dinucleotide phosphate, RFNR2, ST2133, TgFNR, TPNH-ferredoxin reductase, YumC
ECTree
1.18.1.2 ferredoxin-NADP+ reductaseAdvanced search results
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results (Turnover Number
Turnover Number on EC 1.18.1.2 - ferredoxin-NADP+ reductase
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TURNOVER NUMBER [1/s] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.43
reduced 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone
-
at pH 7.5 and 22°C
-
19
reduced flavodoxin mutant I59A
-
using cytochrome c as electron acceptor, for mutant I59A
-
15.3
reduced flavodoxin mutant I59A/I92A
-
using cytochrome c as electron acceptor, for mutant I59A/I92A
-
27.5
reduced flavodoxin mutant I59E
-
using cytochrome c as electron acceptor, for mutant I59E
-
14
reduced flavodoxin mutant I59E/I92E
-
using cytochrome c as electron acceptor, for mutant I59E/I92E
-
25.8
reduced flavodoxin mutant I92A
-
using cytochrome c as electron acceptor, for mutant I92A
-
26.5
reduced flavodoxin mutant I92E
-
using cytochrome c as electron acceptor, for mutant I92E
-
13.8
reduced flavodoxin mutant W57E
-
using cytochrome c as electron acceptor, for mutant W57E
-
90.3
reduced flavodoxin mutant W57K
-
using cytochrome c as electron acceptor, for mutant W57K
-
52.7
reduced flavodoxin mutant W57R
-
using cytochrome c as electron acceptor, for mutant W57R
-
21
2,6-dichlorophenolindophenol
-
recombinant enzyme, pH 8.2, 25°C, with NADH
25.6
2,6-dichlorophenolindophenol
-
recombinant enzyme, pH 8.2, 25°C, with NADPH
3
Fe(III)-EDTA
in the presence of 0.15 mM Fe(III)-EDTA, in the absence of free flavin, in 50 mM sodium phosphate (pH 7.0), at 25°C
3.53
Fe(III)-EDTA
in the presence of 0.15 mM Fe(III)-EDTA, in the presence of 0.15 mM FAD, in 50 mM sodium phosphate (pH 7.0), at 25°C
0.0005
NADH
mutant T155G/A160T/S223D/Y235F/L263P/R264P/G265P, called AMP2PP5
1.16
NADH
-
for FprA in a flavin free assay, using K3Fe(CN)6 as electron acceptor
3.03
NADH
-
for FprA in a flavin free assay, using 2,6-dichlorophenolindophenol as electron acceptor
3.09
NADH
-
for FprB in a flavin free assay, using K3Fe(CN)6 as electron acceptor
3.11
NADH
-
for FprA in a flavin free assay, using Fe(III)-citrate as electron acceptor
4.59
NADH
-
for FprB in a flavin free assay, using 2,6-dichlorophenolindophenol as electron acceptor
5
NADH
mutant with additional tryptophan residue at the C-terminus, pH 8.0, 30°C
5.6
NADH
-
for FprA in a flavin free assay, using Fe(III)-EDTA as electron acceptor
7.71
NADH
-
for FprA with FMN as cofactor, using Fe(III)-citrate as electron acceptor
8.21
NADH
-
for FprB in a flavin free assay, using Fe(III)-EDTA as electron acceptor
9.18
NADH
-
for FprA with FMN as cofactor, using Fe(III)-EDTA as electron acceptor
10
NADH
-
for FprA with FAD as cofactor, using Fe(III)-citrate as electron acceptor
10.18
NADH
-
for FprA with FAD as cofactor, using Fe(III)-EDTA as electron acceptor
10.64
NADH
-
for FprB in a flavin free assay, using Fe(III)-citrate as electron acceptor
13.2
NADH
-
for FprB with FAD as cofactor, using Fe(III)-EDTA as electron acceptor
16.44
NADH
-
for FprB with FMN as cofactor, using Fe(III)-citrate as electron acceptor
17.47
NADH
-
for FprB with FMN as cofactor, using Fe(III)-EDTA as electron acceptor
19.24
NADH
-
for FprB with FAD as cofactor, using Fe(III)-citrate as electron acceptor
45.3
NADH
mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C
0.24
NADPH
-
pH 7.4, temperature not specified in the publication, recombinant enzyme
0.6
NADPH
-
pH 8.2, temperature not specified in the publication, recombinant enzyme
1
NADPH
mutant Del267-272, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C
1.91
NADPH
-
for FprB in a flavin free assay, using Fe(III)-EDTA as electron acceptor
3.2
NADPH
with 2,6-dichlorophenolindophenol as cosubstrate, at pH 7.0 and 25°C
3.8
NADPH
in an assay using K3Fe(CN)6 as electron acceptor for mutant H286K
3.82
NADPH
-
for FprB in a flavin free assay, using K3Fe(CN)6 as electron acceptor
4.51
NADPH
-
for FprB in a flavin free assay, using 2,6-dichlorophenolindophenol as electron acceptor
4.77
NADPH
-
for FprA in a flavin free assay, using 2,6-dichlorophenolindophenol as electron acceptor
5.99
NADPH
-
for FprA in a flavin free assay, using K3Fe(CN)6 as electron acceptor
6
NADPH
in an assay using 2,6-dichlorophenolindophenol as electron acceptor for mutant H286K
6.18
NADPH
-
for FprA in a flavin free assay, using Fe(III)-EDTA as electron acceptor
6.8
NADPH
-
for FprA with FAD as cofactor, using Fe(III)-EDTA as electron acceptor
7
NADPH
mutant A266Y, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C
7.13
NADPH
-
for FprA in a flavin free assay, using Fe(III)-citrate as electron acceptor
7.5
NADPH
in an assay using K3Fe(CN)6 as electron acceptor for mutant H286L
7.54
NADPH
-
for FprA with FAD as cofactor, using Fe(III)-citrate as electron acceptor
8
NADPH
mutant Del267-272, substrate ferricyanide, pH 7.2, 25°C
10.1
NADPH
-
mutant bearing an artificial metal binding site of nine amino acids at the C-terminus, presence of Zn2+, 30°C, pH 8.0
10.28
NADPH
-
for FprB with FAD as cofactor, using Fe(III)-EDTA as electron acceptor
10.77
NADPH
-
for FprB with FAD as cofactor, using Fe(III)-citrate as electron acceptor
11.18
NADPH
-
for FprA with FMN as cofactor, using Fe(III)-EDTA as electron acceptor
11.92
NADPH
-
for FprB in a flavin free assay, using Fe(III)-citrate as electron acceptor
12
NADPH
mutant A266Y/Del267-272, substrate ferricyanide, pH 7.2, 25°C
17.5
NADPH
in an assay using 2,6-dichlorophenolindophenol as electron acceptor for mutant H286A
20
NADPH
wild-type, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C
20.38
NADPH
-
for FprB with FMN as cofactor, using Fe(III)-EDTA as electron acceptor
21.71
NADPH
-
pH 6.8, temperature not specified in the publication, recombinant enzyme
21.72
NADPH
-
for FprB with FMN as cofactor, using Fe(III)-citrate as electron acceptor
22.6
NADPH
-
with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 8.0 and 25°C
24.5
NADPH
mutant with an insertion of the iloop of Pisum sativum enzyme, pH 8.0, 30°C
37.61
NADPH
-
for FprA with FMN as cofactor, using Fe(III)-citrate as electron acceptor
44.5
NADPH
in an assay using K3Fe(CN)6 as electron acceptor for mutant H286A
55
NADPH
in an assay using 2,6-dichlorophenolindophenol as electron acceptor
56.1
NADPH
-
enzyme in soluble extract, with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 8.0, temperature not specified in the publication
59
NADPH
-
recombinant mutant E139K, diaphorase activity with 2,6-dichlorophenolindophenol, pH 8.0, 25°C, ionic strength of 28 mM
65
NADPH
using 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium chloride as electron acceptor
70
NADPH
in an assay using 2,6-dichlorophenolindophenol as electron acceptor for mutant H286Q
73.5
NADPH
-
mutant bearing an artificial metal binding site of nine amino acids at the C-terminus, absence of Zn2+, 30°C, pH 8.0
81
NADPH
-
recombinant wild-type enzyme, diaphorase activity with 2,6-dichlorophenolindophenol, pH 8.0, 25°C, ionic strength of 28 mM
86
NADPH
-
enzyme in PBS, with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 8.0, temperature not specified in the publication
88
NADPH
-
recombinant mutant E139Q, diaphorase activity with 2,6-dichlorophenolindophenol, pH 8.0, 25°C, ionic strength of 28 mM
89
NADPH
-
recombinant mutant E139D, diaphorase activity with 2,6-dichlorophenolindophenol, pH 8.0, 25°C, ionic strength of 28 mM
99
NADPH
mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C
121.9
NADPH
pH 8.0, temperature not specified in the publication
185
NADPH
in an assay using K3Fe(CN)6 as electron acceptor for mutant H286Q
213
NADPH
-
with 2 mM ferricyanide in 20 mM HEPES-NaOH buffer, at pH 7.0 and 25°C
225
NADPH
-
electron transfer via the enzyme to oxidized ferredoxin and further to cytochrome c
250
NADPH
-
electron transfer via the enzyme to oxidized ferredoxin and further to cytochrome c
360.5
NADPH
mutant with additional tryptophan residue at the C-terminus, pH 8.0, 30°C
520
NADPH
-
electron transfer via the enzyme to oxidized ferredoxin and further to cytochrome c
3.7
oxidized ferredoxin
mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C
19.4
oxidized ferredoxin
mutant with an insertion of the iloop of Pisum sativum enzyme, pH 8.0, 30°C
35.9
oxidized ferredoxin
mutant with additional tryptophan residue at the C-terminus, pH 8.0, 30°C
16.5
oxidized [2Fe-2S]-[rubredoxin]
cosubstrate NADH, pH 7, 25°C
-
24.8
oxidized [2Fe-2S]-[rubredoxin]
cosubstrate NADPH, pH 7, 25°C
-
58
reduced ferredoxin
-
recombinant mutant E139Q, pH 8.0, 25°C, ionic strength of 100 mM
70
reduced ferredoxin
-
recombinant mutant E139Q, pH 8.0, 25°C, ionic strength of 200 mM
117
reduced ferredoxin
-
recombinant mutant E139Q, pH 8.0, 25°C, ionic strength of 28 mM
120
reduced ferredoxin
-
recombinant mutant E139K, pH 8.0, 25°C, ionic strength of 200 mM
135
reduced ferredoxin
-
recombinant wild-type enzyme, pH 8.0, 25°C, ionic strength of 200 mM
148
reduced ferredoxin
-
recombinant mutant E139D, pH 8.0, 25°C, ionic strength of 200 mM
155
reduced ferredoxin
-
recombinant mutant E139K, pH 8.0, 25°C, ionic strength of 100 mM
176
reduced ferredoxin
-
recombinant mutant E139K, pH 8.0, 25°C, ionic strength of 28 mM
192
reduced ferredoxin
-
recombinant mutant E139D, pH 8.0, 25°C, ionic strength of 100 mM
209
reduced ferredoxin
-
recombinant wild-type enzyme, pH 8.0, 25°C, ionic strength of 100 mM
225
reduced ferredoxin
-
recombinant wild-type enzyme, pH 8.0, 25°C, ionic strength of 28 mM
280
reduced ferredoxin
-
recombinant mutant E139D, pH 8.0, 25°C, ionic strength of 28 mM
2 - 8
reduced flavodoxin
-
recombinant mutant E139K, pH 8.0, 25°C, ionic strength of 200 mM
14
reduced flavodoxin
-
recombinant wild-type enzyme, pH 8.0, 25°C, ionic strength of 200 mM
17
reduced flavodoxin
-
recombinant mutant E139K, pH 8.0, 25°C, ionic strength of 28 mM
19
reduced flavodoxin
-
recombinant wild-type enzyme, pH 8.0, 25°C, ionic strength of 100 mM
20
reduced flavodoxin
-
recombinant mutant E139Q, pH 8.0, 25°C, ionic strength of 200 mM
24
reduced flavodoxin
-
recombinant wild-type enzyme, pH 8.0, 25°C, ionic strength of 28 mM
25
reduced flavodoxin
-
recombinant mutant E139Q, pH 8.0, 25°C, ionic strength of 100 mM
25
reduced flavodoxin
-
recombinant mutant E139Q, pH 8.0, 25°C, ionic strength of 28 mM
26
reduced flavodoxin
-
recombinant mutant E139K, pH 8.0, 25°C, ionic strength of 100 mM
38
reduced flavodoxin
-
recombinant mutant E139D, pH 8.0, 25°C, ionic strength of 28 mM
38.1
reduced flavodoxin
-
mutant bearing a truncated N-terminal domain beginning after the KISKK domain, pH 7.5, temperature not specified in the publication
45.4
reduced flavodoxin
-
mutant bearing lysine to glutamine mutations in the second and third lysine residues of the KISKK domain, pH 7.5, temperature not specified in the publication
65
reduced flavodoxin
-
mutant bearing a lysine to glutamine mutation in the first lysine residue of the KISKK domain, pH 7.5, temperature not specified in the publication
66.3
reduced flavodoxin
-
mutant bearing a lysine to glutamine mutation in the second lysine residue of the KISKK domain, pH 7.5, temperature not specified in the publication
104
reduced flavodoxin
-
wild-type, pH 7.5, temperature not specified in the publication
128.2
reduced flavodoxin
-
mutant bearing an N-terminal region with the full wheat KISKK domain, pH 7.5, temperature not specified in the publication
139.4
reduced flavodoxin
-
mutant with an extended N-terminal region to include the EAxxPA motif of maize, pH 7.5, temperature not specified in the publication
additional information
additional information
-
the low efficiency is intrinsic to the reductase itself
-
