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Information on EC 1.19.1.1 - flavodoxin-NADP+ reductase and Organism(s) Nostoc sp. and UniProt Accession P21890

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IUBMB Comments
A flavoprotein (FAD). This activity occurs in some prokaryotes and algae that possess flavodoxin, and provides low-potential electrons for a variety of reactions such as nitrogen fixation, sulfur assimilation and amino acid biosynthesis. In photosynthetic organisms it is involved in the photosynthetic electron transport chain. The enzyme also catalyses EC 1.18.1.2, ferredoxin---NADP+ reductase.
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This record set is specific for:
Nostoc sp.
UNIPROT: P21890
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The taxonomic range for the selected organisms is: Nostoc sp.
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
Bc_0385, ferredoxin (flavodoxin):NADP+ oxidoreductase, ferredoxin/flavodoxin-NADP(H) oxidoreductase, FLDR, FNR, FPR, PETH, YumC, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
flavodoxin:NADP+ oxidoreductase
A flavoprotein (FAD). This activity occurs in some prokaryotes and algae that possess flavodoxin, and provides low-potential electrons for a variety of reactions such as nitrogen fixation, sulfur assimilation and amino acid biosynthesis. In photosynthetic organisms it is involved in the photosynthetic electron transport chain. The enzyme also catalyses EC 1.18.1.2, ferredoxin---NADP+ reductase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
show the reaction diagram
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-
-
?
additional information
?
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no changes are found in the kinetics of reduction of the FMN cofactor of flavodoxin modified by glycine ethyl ester as compared with the native protein. The observed rate constants for reoxidation of ferredoxin by FNR (reaction of EC 1.18.1.2) are about 100fold decreased when phenylglyoxal-modified FNR is used. When phenylglyoxal-modified FNR is used to reduce flavodoxin, similar inhibitory effects are observed. In this case, the limiting first-order rate constant for flavodoxin semiquinone formation via intracomplex electron transfer is approximately 12fold smaller than that obtained for the native FNR. Ionic strength effects are diminished. Complex formation can still occur between modified FNR and native flavodoxin, and between native FNR and modified flavodoxin, but the geometry of these complexes is altered so as to decrease the effectiveness of interprotein electron transfer
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
reduction of the FAD moiety of phenylglyoxal-modified FNR by laser-generated 5-deazariboflavin semiquinone occurs with a second-order rate constant 2.5fold smaller than that obtained for reduction of native FNR
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.033 - 0.043
reduced flavodoxin
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.5 - 23.3
reduced flavodoxin
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
170 - 700
reduced flavodoxin
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the C-terminal tyrosine residue lowers the affinity for NADP(H) to levels compatible with steady-state turnover, contributes to the flavin semiquinone stabilization required for electron splitting, and modulates the rates of electron exchange with the protein partners
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a multiscale modelling approach for analysis of the electron transfer process in complexes of the enzyme with both ferredoxin and flavodoxin, reactions of EC 1.19.1.1 and EC1.18.1.2, respectively. The electron transfer in FNR/ferredoxin proceedes through a bridge-mediated mechanism in a dominant protein-protein complex, where transfer of the electron is facilitated by ferredoxin loop-residues 40-49. In FNR/flavodoxin, a direct transfer between redox cofactors is observed and less complex specificity than in ferredoxin
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y303F
about 30% of the wild-type enzyme activity with ferredoxin, about 25% of the wild-type enzyme activity with flavodoxin
Y303S
inactive. Mutation shifts the flavin reduction potential to less negative values, whereas semiquinone stabilization is severely hampered
Y303W
almost inactive
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nogues, I.; Tejero, J.; Hurley, J.K.; Paladini, D.; Frago, S.; Tollin, G.; Mayhew, S.G.; Gomez-Moreno, C.; Ceccarelli, E.A.; Carrillo, N.; Medina, M.
Role of the C-terminal tyrosine of ferredoxin-nicotinamide adenine dinucleotide phosphate reductase in the electron transfer processes with its protein partners ferredoxin and flavodoxin
Biochemistry
43
6127-6137
2004
Nostoc sp. (P21890), Nostoc sp. ATCC 29151 (P21890), Pisum sativum (P10933)
Manually annotated by BRENDA team
Saen-Oon, S.; Cabeza De Vaca, I.; Masone, D.; Medina, M.; Guallar, V.
A theoretical multiscale treatment of protein-protein electron transfer: The ferredoxin/ferredoxin-NADP+ reductase and flavodoxin/ferredoxin-NADP+ reductase systems
Biochim. Biophys. Acta
1847
1530-1538
2015
Nostoc sp. (P21890), Nostoc sp. ATCC 29151 (P21890)
Manually annotated by BRENDA team
Medina, M.; Gomez-Moreno, C.; Tollin, G.
Effects of chemical modification of Anabaena flavodoxin and ferredoxin-NADP+ reductase on the kinetics of interprotein electron transfer reactions
Eur. J. Biochem.
210
577-583
1992
Nostoc sp. (P21890), Nostoc sp. ATCC 29151 (P21890)
Manually annotated by BRENDA team