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
-
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
- 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
results (
results (KM Value
KM Value on EC 1.18.1.2 - ferredoxin-NADP+ reductase
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.095
2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyltetrazolium chloride
at 25°C in 200 mM Tris-HCl (pH 9.0), containing 70 mM NaCl and 0.1% Triton-X100
0.03 - 0.0547
iodonitrotetrazolium violet
-
4 different fractions after ferredoxin-Sepharose chromatography
0.46
reduced 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone
-
at pH 7.5 and 22°C
-
0.00364
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
0.0396
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
0.00205
ferricytochrome c
-
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
0.00312
ferricytochrome c
-
wild-type, pH 7.5, temperature not specified in the publication
0.0035
ferricytochrome c
-
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
0.00999
ferricytochrome c
-
mutant bearing an N-terminal region with the full wheat KISKK domain, pH 7.5, temperature not specified in the publication
0.0103
ferricytochrome c
-
mutant bearing a truncated N-terminal domain beginning after the KISKK domain, pH 7.5, temperature not specified in the publication
0.0104
ferricytochrome c
-
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
0.01103
ferricytochrome c
-
mutant with an extended N-terminal region to include the EAxxPA motif of maize, pH 7.5, temperature not specified in the publication
0.00112
NADH
-
for FprB in a cytochrome c assay, using Pseudomonas putida [4Fe-4S]-ferredoxin FdxA as electron acceptor
0.00235
NADH
-
for FprB with FMN as cofactor, using Fe(III)-citrate as electron acceptor
0.00273
NADH
-
for FprA with FMN as cofactor, using Fe(III)-citrate as electron acceptor
0.00298
NADH
-
for FprB in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdA as electron acceptor
0.003
NADH
mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C
0.00338
NADH
-
for FprB in a flavin free assay, using Fe(III)-citrate as electron acceptor
0.00464
NADH
-
for FprB in a flavin free assay, using K3Fe(CN)6 as electron acceptor
0.0059
NADH
mutant with additional tryptophan residue at the C-terminus, pH 8.0, 30°C
0.00616
NADH
-
for FprB with FAD as cofactor, using Fe(III)-citrate as electron acceptor
0.0065
NADH
-
for FprB with FMN as cofactor, using Fe(III)-EDTA as electron acceptor
0.007
NADH
-
for FprB in a flavin free assay, using Fe(III)-EDTA as electron acceptor
0.00717
NADH
-
for FprB in a flavin free assay, using 2,6-dichlorophenolindophenol as electron acceptor
0.00802
NADH
-
for FprB in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdB as electron acceptor
0.00822
NADH
-
for FprB in a cytochrome c assay, using Pseudomonas putida flavodoxin Fld as electron acceptor
0.00866
NADH
-
for FprA with FMN as cofactor, using Fe(III)-EDTA as electron acceptor
0.00933
NADH
-
for FprA in a cytochrome c assay, using Pseudomonas putida [4Fe-4S]-ferredoxin FdxA as electron acceptor
0.00943
NADH
-
for FprA in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdB as electron acceptor
0.01063
NADH
-
for FprA in a flavin free assay, using K3Fe(CN)6 as electron acceptor
0.01163
NADH
-
for FprA in a cytochrome c assay, using Pseudomonas putida flavodoxin Fld as electron acceptor
0.01238
NADH
-
for FprA with FAD as cofactor, using Fe(III)-citrate as electron acceptor
0.0129
NADH
-
for FprB with FAD as cofactor, using Fe(III)-EDTA as electron acceptor
0.01866
NADH
-
for FprA with FAD as cofactor, using Fe(III)-EDTA as electron acceptor
0.02363
NADH
-
for FprA in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdA as electron acceptor
0.05625
NADH
-
for FprA in a flavin free assay, using Fe(III)-EDTA as electron acceptor
0.0632
NADH
-
for FprA in a flavin free assay, using 2,6-dichlorophenolindophenol as electron acceptor
0.1076
NADH
-
for FprA in a flavin free assay, using Fe(III)-citrate as electron acceptor
0.72
NADH
with K3Fe(CN)6 as cosubstrate, at 25°C, in 100 mM Tris-HCl (pH 8.2)
1.25
NADH
mutant T155G/A160T/S223D/Y235F/L263P/R264P/G265P, called AMP2PP5
0.00083
NADPH
-
for FprA in a cytochrome c assay, using Pseudomonas putida flavodoxin Fld as electron acceptor
0.00089
NADPH
-
recombinant enzyme, pH 8.2, 25°C, with 2,6-dichlorophenolindophenol
0.00111
NADPH
-
for FprB in a cytochrome c assay, using Pseudomonas putida [4Fe-4S]-ferredoxin FdxA as electron acceptor
0.0016
NADPH
with 2,6-dichlorophenolindophenol as cosubstrate, at pH 7.0 and 25°C
0.0018
NADPH
in the presence of 0.15 mM Fe(III)-EDTA, in 50 mM sodium phosphate (pH 7.0), at 25°C
0.00181
NADPH
-
for FprB in a cytochrome c assay, using Pseudomonas putida flavodoxin Fld as electron acceptor
0.00191
NADPH
-
for FprA in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdA as electron acceptor
0.00191
NADPH
-
for FprA in a cytochrome c assay, using Pseudomonas putida [4Fe-4S]-ferredoxin FdxA as electron acceptor
0.0024
NADPH
-
mutant bearing an artificial metal binding site of nine amino acids at the C-terminus, absence of Zn2+, 30°C, pH 8.0
0.00245
NADPH
-
for FprA in a flavin free assay, using K3Fe(CN)6 as electron acceptor
0.0026
NADPH
-
mutant bearing an artificial metal binding site of nine amino acids at the C-terminus, presence of Zn2+, 30°C, pH 8.0
0.00263
NADPH
-
for FprB in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdA as electron acceptor
0.003
NADPH
mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C
0.00326
NADPH
-
for FprB in a flavin free assay, using K3Fe(CN)6 as electron acceptor
0.0034
NADPH
-
recombinant mutant E139Q, diaphorase activity with 2,6-dichlorophenolindophenol, pH 8.0, 25°C, ionic strength of 28 mM
0.0036
NADPH
mutant with an insertion of the iloop of Pisum sativum enzyme, pH 8.0, 30°C
0.0037
NADPH
-
pH 7.4, temperature not specified in the publication, recombinant enzyme
0.00397
NADPH
-
for FprB in a flavin free assay, using 2,6-dichlorophenolindophenol as electron acceptor
0.004
NADPH
in a ferredoxin-dependent cytochrome c reduction assay
0.00457
NADPH
-
for FprA in a flavin free assay, using Fe(III)-EDTA as electron acceptor
0.00459
NADPH
-
for FprA in a flavin free assay, using Fe(III)-citrate as electron acceptor
0.0047
NADPH
-
recombinant mutant E139D, diaphorase activity with 2,6-dichlorophenolindophenol, pH 8.0, 25°C, ionic strength of 28 mM
0.00479
NADPH
-
for FprA in a flavin free assay, using 2,6-dichlorophenolindophenol as electron acceptor
0.0058
NADPH
-
recombinant mutant E139K, diaphorase activity with 2,6-dichlorophenolindophenol, pH 8.0, 25°C, ionic strength of 28 mM
0.00587
NADPH
-
for FprB in a flavin free assay, using Fe(III)-citrate as electron acceptor
0.006
NADPH
-
recombinant wild-type enzyme, diaphorase activity with 2,6-dichlorophenolindophenol, pH 8.0, 25°C, ionic strength of 28 mM
0.00615
NADPH
-
for FprA in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdB as electron acceptor
0.00625
NADPH
-
for FprA with FMN as cofactor, using Fe(III)-citrate as electron acceptor
0.00636
NADPH
-
for FprA with FAD as cofactor, using Fe(III)-citrate as electron acceptor
0.0066
NADPH
-
with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 8.0 and 25°C
0.00666
NADPH
-
for FprA with FMN as cofactor, using Fe(III)-EDTA as electron acceptor
0.00686
NADPH
-
for FprB in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdB as electron acceptor
0.0074
NADPH
-
pH 7.0, 15°C, recombinant chimeric enzyme, diaphorase activity
0.00751
NADPH
-
for FprA with FAD as cofactor, using Fe(III)-EDTA as electron acceptor
0.009
NADPH
mutant Del267-272, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C
0.0094
NADPH
-
pH 8.2, temperature not specified in the publication, recombinant enzyme
0.0108
NADPH
pH 8.0, temperature not specified in the publication
0.011 - 0.035
NADPH
-
ferredoxin-dependent cytochrome c reductase activity
0.01177
NADPH
-
for FprB with FAD as cofactor, using Fe(III)-citrate as electron acceptor
0.0125
NADPH
-
enzyme in PBS, with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 8.0, temperature not specified in the publication
0.01319
NADPH
-
for FprB with FMN as cofactor, using Fe(III)-citrate as electron acceptor
0.0142
NADPH
-
with 2 mM ferricyanide in 20 mM HEPES-NaOH buffer, at pH 7.0 and 25°C
0.01424
NADPH
-
for FprB with FAD as cofactor, using Fe(III)-EDTA as electron acceptor
0.01544
NADPH
-
for FprB with FMN as cofactor, using Fe(III)-EDTA as electron acceptor
0.0163
NADPH
-
enzyme in soluble extract, with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 8.0, temperature not specified in the publication
0.02
NADPH
mutant Del267-272, substrate ferricyanide, pH 7.2, 25°C
0.0207
NADPH
mutant with additional tryptophan residue at the C-terminus, pH 8.0, 30°C
0.022
NADPH
in an assay using 2,6-dichlorophenolindophenol as electron acceptor for mutant H286Q
0.0242
NADPH
-
pH 6.8, temperature not specified in the publication, recombinant enzyme
0.02967
NADPH
-
for FprB in a flavin free assay, using Fe(III)-EDTA as electron acceptor
0.033 - 0.062
NADPH
-
NADPH-2,6-dichlorophenol indophenol diaphorase activity
0.036
NADPH
with K3Fe(CN)6 as cosubstrate, at 25°C, in 100 mM Tris-HCl (pH 8.2)
0.039
NADPH
mutant A266Y/Del267-272, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C
0.043
NADPH
mutant A266Y, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C
0.043
NADPH
mutant A266Y/Del267-272, substrate ferricyanide, pH 7.2, 25°C
0.05
NADPH
using 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium chloride as electron acceptor
0.057
NADPH
in an assay using K3Fe(CN)6 as electron acceptor for mutant H286Q
0.071
NADPH
in an assay using 2,6-dichlorophenolindophenol as electron acceptor
0.085
NADPH
wild-type, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C
0.14
NADPH
in an assay using 2,6-dichlorophenolindophenol as electron acceptor for mutant H286K
0.35
NADPH
cosubstrate 2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyltetrazolium chloride, 25°C, pH 9.0
0.35
NADPH
with 2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyltetrazolium chloride as cosubstrate, at 25°C, in 100 mM Tris-HCl (pH 8.2)
0.37
NADPH
in an assay using K3Fe(CN)6 as electron acceptor for mutant H286L
0.4
NADPH
in an assay using 2,6-dichlorophenolindophenol as electron acceptor for mutant H286A
0.52
NADPH
in an assay using K3Fe(CN)6 as electron acceptor for mutant H286A
1.8
NADPH
above, mutant T155G/A160T/S223D/R224Q/R233L/Y235F/L263P, pH 8.0
0.036
oxidized 2,6-dichlorophenolindophenol
-
diaphorase activity enzyme I
0.047
oxidized 2,6-dichlorophenolindophenol
-
diaphorase activity enzyme II
0.068
oxidized 2,6-dichlorophenolindophenol
-
recombinant enzyme, pH 8.2, 25°C, with Fe(CN)63-
0.083
oxidized 2,6-dichlorophenolindophenol
-
recombinant enzyme, pH 8.2, 25°C, with 2,6-dichlorophenolindophenol
0.00027
oxidized ferredoxin
-
recombinant mutant E139Q, pH 8.0, 25°C, ionic strength of 28 mM
0.0005
oxidized ferredoxin
-
recombinant mutant E139Q, pH 8.0, 25°C, ionic strength of 100 mM
0.0008
oxidized ferredoxin
Plasmodium falciparum ferredoxin PfFd is tested;using cytochrome c as electron acceptor
0.0009
oxidized ferredoxin
-
recombinant mutant E139Q, pH 8.0, 25°C, ionic strength of 200 mM
0.0009
oxidized ferredoxin
mutant lacking the beta-hairpin, pH 8.0, 30°C
0.0009
oxidized ferredoxin
mutant with additional tryptophan residue at the C-terminus, pH 8.0, 30°C
0.0018
oxidized ferredoxin
mutant with an insertion of the iloop of Pisum sativum enzyme, pH 8.0, 30°C
0.0025
oxidized ferredoxin
-
recombinant mutant E139K, pH 8.0, 25°C, ionic strength of 100 mM
0.0035
oxidized ferredoxin
-
recombinant mutant E139K, pH 8.0, 25°C, ionic strength of 200 mM
0.0043
oxidized ferredoxin
-
recombinant mutant E139K, pH 8.0, 25°C, ionic strength of 28 mM
0.0076
oxidized ferredoxin
mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C
0.02
oxidized ferredoxin
-
recombinant wild-type enzyme, pH 8.0, 25°C, ionic strength of 100 mM
0.021
oxidized ferredoxin
-
recombinant wild-type enzyme, pH 8.0, 25°C, ionic strength of 200 mM
0.023
oxidized ferredoxin
-
recombinant mutant E139D, pH 8.0, 25°C, ionic strength of 100 mM
0.023
oxidized ferredoxin
-
recombinant wild-type enzyme, pH 8.0, 25°C, ionic strength of 28 mM
0.1
oxidized ferredoxin
-
recombinant mutant E139D, pH 8.0, 25°C, ionic strength of 28 mM
0.4
oxidized ferredoxin
-
recombinant mutant E139D, pH 8.0, 25°C, ionic strength of 200 mM
0.0195
oxidized [2Fe-2S]-[rubredoxin]
cosubstrate NADH, pH 7, 25°C
-
0.021
oxidized [2Fe-2S]-[rubredoxin]
cosubstrate NADPH, pH 7, 25°C
-
0.032
oxidized [2Fe-2S]-[rubredoxin]
cosubstrate NADPH, pH 7, 25°C
-
0.01 - 0.016
reduced 2,6-dichlorophenolindophenol
-
NADPH-2,6-dichlorophenol-indophenol diaphorase activity
0.056
reduced 2,6-dichlorophenolindophenol
-
recombinant enzyme, pH 8.2, 25°C, with NADH
0.058
reduced 2,6-dichlorophenolindophenol
-
recombinant enzyme, pH 8.2, 25°C, with NADPH
0.0028
reduced ferredoxin
-
mutant lacking amino acids 81 to 118, pH 8.2, 25°C
0.0045 - 0.0046
reduced ferredoxin
-
ferredoxin-dependent cytochrome c reductase activity
additional information
additional information
-
increasing NH4Cl concentration enhances Km
-
additional information
additional information
-
enzyme reacts slower with different mutants of ferredoxin than with wild type ferredoxin
-
additional information
additional information
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Km value increases with pH
-
additional information
additional information
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Km value increases with pH
-
additional information
additional information
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Km value increases with pH
-
additional information
additional information
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Km value increases with pH
-
additional information
additional information
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Km value increases with pH
-
additional information
additional information
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Km value increases with pH
-
additional information
additional information
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Km value increases with pH
-
additional information
additional information
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Km value increases with pH
-
additional information
additional information
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Km value increases with pH
-
additional information
additional information
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Km value increases with pH
-
additional information
additional information
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Km value increases with pH
-
additional information
additional information
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Km value increases with pH
-
additional information
additional information
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Km value increases with pH
-
additional information
additional information
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enzyme covalently cross-linked to flavodoxin
-
additional information
additional information
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increasing light intensity reduces Km
-
additional information
additional information
kinetics, wild-type and mutant enzymes
-
additional information
additional information
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Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
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below 0.1 mM, oxidized ferredoxin with NADH, pH 7.0, 24°C
-
additional information
additional information
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detailed binding kinetics, detailed reaction kinetics, enzyme-substrate complex formation
-
additional information
additional information
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forward and reverse reactions follow different kinetic mechanism, overview
-
additional information
additional information
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forward and reverse reactions follow different kinetic mechanism, overview
-
additional information
additional information
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forward and reverse reactions follow different kinetic mechanism, overview
-
additional information
additional information
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forward and reverse reactions follow different kinetic mechanism, overview
-
additional information
additional information
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forward and reverse reactions follow different kinetic mechanism, overview
-
additional information
additional information
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forward and reverse reactions follow different kinetic mechanism, overview
-
additional information
additional information
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forward and reverse reactions follow different kinetic mechanism, overview
-
additional information
additional information
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forward and reverse reactions follow different kinetic mechanism, overview
-
additional information
additional information
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gradual decrease in activity according to biphasic kinetics within 120 min
-
additional information
additional information
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kinetics, rapid thermal inactivation of reduced enzyme and drop of activity
-
additional information
additional information
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steady-state kinetics and dissociation constants of NADPH-enzyme complex, wild-type isozymes and recombinant chimera
-
additional information
additional information
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stopped-flow and laser flash kinetic measurements, steady-state kinetics, dissociation constants and reduction potentials of wild-type and mutant enzymes
-
additional information
additional information
stopped-flow and laser flash kinetic measurements, steady-state kinetics, dissociation constants and reduction potentials of wild-type and mutant enzymes
-
additional information
additional information
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stopped-flow kinetics measurements, pH 8.0, 13°C, steady-state kinetics for wild-type and mutant enzymes dependent on ionic strength, overview
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additional information
additional information
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thermodynamics and kinetics, measurement of direct electron transfer by stopped-flow spectrophotometry
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additional information
additional information
thermodynamics and kinetics, measurement of direct electron transfer by stopped-flow spectrophotometry
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additional information
additional information
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Michaelis-Menten kinetics, overview
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additional information
additional information
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analysis of kinetic rate constants for the reaction of enzyme with NADP+/NADPH
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additional information
additional information
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Fpr showed high specificity for NADPH; Km value for NADPH is <5 microMol, whereas that for NADH is above 2 mM
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additional information
additional information
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Stopped-flow pre-steady-state kinetics, overview
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additional information
additional information
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kinetic evidence for its bifurcating behavior of the enzyme, cofactor kinetics, overview
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additional information
additional information
spectroscopic steady-state and dynamic kinetics of wild-type and mutant DELTAA266, DELTAA266Y, and A266Y enzymes, detailed overview
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additional information
additional information
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spectroscopic steady-state and dynamic kinetics of wild-type and mutant DELTAA266, DELTAA266Y, and A266Y enzymes, detailed overview
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