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Information on EC 1.5.1.40 - 8-hydroxy-5-deazaflavin:NADPH oxidoreductase
for references in articles please use BRENDA:EC1.5.1.40
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EC Tree 1 Oxidoreductases
1.5 Acting on the CH-NH group of donors
1.5.1 With NAD+ or NADP+ as acceptor
1.5.1.40 8-hydroxy-5-deazaflavin:NADPH oxidoreductase
IUBMB Comments
The enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate .
The expected taxonomic range for this enzyme is: Bacteria, Archaea
- 1.5.1.40
-
methanogen
- archaea
-
hydride
- 8-hydroxy-5-deazaflavins
-
methanococcus
- hydrogenase
- vannielii
- thermoautotrophicum
-
methanobacterium
-
methanobrevibacter
- griseus
-
methanogenesis
-
stereochemical
- smithii
-
si-face
- methane
- fulgidus
- ch4
showSynonyms
8-hydroxy-5-deazaflavin-dependent nadp+ reductase, tfu-fno, f420-dependent nadp reductase, f420h2:nadp oxidoreductase, nadp+:f420 oxidoreductase, f420-dependent nadp oxidoreductase, 8-hydroxy-5-deazaflavin:nadph oxidoreductase, f420h2:nadp+ oxidoreductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
8-hydroxy-5-deazaflavin-dependent NADP+ reductase
8-OH-5-deazaflavin:NADPH oxidoreductase
F420-dependent NADP oxidoreductase
F420-dependent NADP reductase
F420H2:NADP oxidoreductase
Fno
Msm_0049
NADP+:F420 oxidoreductase
8-hydroxy-5-deazaflavin-dependent NADP+ reductase
-
the enzyme is a component of the formate NADP+ oxidoreductase system of Methanococcus vannielii
8-hydroxy-5-deazaflavin-dependent NADP+ reductase
-
the enzyme is a component of the formate NADP+ oxidoreductase system of Methanococcus vannielii
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reduced coenzyme F420 + NADP+ = oxidized coenzyme F420 + NADPH + H+
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
reduced coenzyme F420:NADP+ oxidoreductase
The enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate [1].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5'-O-methyl-7,8-didemethyl-8-hydroxyflavin + NADPH + H+
8-hydroxypyrimido[4,5-b]-2,4-(3H,10H)-dione + NADP+
-
Substrates: the enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate
Products: -
Products: -
r
5-deaza-8-hydroxyisoalloxazine + NADPH + H+
8-hydroxypyrimido[4,5-b]-2,4-(3H,10H)-dione + NADP+
-
Substrates: the enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate
Products: -
Products: -
?
7,8-didemethyl-8-hydroxy-5-deazariboflavin 5'-phosphate + NADPH + H+
1-deoxy-1-(8-hydroxy-2,4-dioxo-1,3,4,5-tetrahydropyrimido[4,5-b]quinolin-10(2H)-yl)-5-O-phospho-D-ribitol + NADP+
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Substrates: the enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate
Products: -
Products: -
?
reduced coenzyme F420 + 1-aminoethylnicotinamide
oxidized coenzyme F420 + ?
Substrates: -
Products: -
Products: -
?
reduced coenzyme F420 + 1-benzyl-3-acetylpyridine
oxidized coenzyme F420 + ?
Substrates: -
Products: -
Products: -
?
reduced coenzyme F420 + 1-benzylnicotinamide
oxidized coenzyme F420 + ?
Substrates: -
Products: -
Products: -
?
reduced coenzyme F420 + 1-ethylnicotinamide
oxidized coenzyme F420 + ?
Substrates: -
Products: -
Products: -
?
reduced coenzyme F420 + 1-hydroxyethylnicotinamide
oxidized coenzyme F420 + ?
Substrates: -
Products: -
Products: -
?
reduced coenzyme F420 + 1-hydroxypropylnicotinamide
oxidized coenzyme F420 + ?
Substrates: -
Products: -
Products: -
?
reduced coenzyme F420 + 1-propylnicotinamide
oxidized coenzyme F420 + ?
Substrates: -
Products: -
Products: -
?
1,5-dihydro-8-hydroxy-5-deazaflavin + NADP+
8-hydroxy-5-deazaflavin + NADPH + H+
-
Substrates: the kcat value of the forward reaction is 24 times greater than that of the reverse reaction, thus the production of NADPH at pH 7.0 is more favorable than its consumption
Products: -
Products: -
r
1,5-dihydro-8-hydroxy-5-deazaflavin + NADP+
8-hydroxy-5-deazaflavin + NADPH + H+
-
Substrates: the kcat value of the forward reaction is 24 times greater than that of the reverse reaction, thus the production of NADPH at pH 7.0 is more favorable than its consumption
Products: -
Products: -
r
5-deaza-8-hydroxy-10-methylisoalloxazine + NADPH + H+
? + NADP+
-
Substrates: -
Products: -
Products: -
?
5-deaza-8-hydroxy-10-methylisoalloxazine + NADPH + H+
? + NADP+
-
Substrates: -
Products: -
Products: -
?
coenzyme F0 + NADPH + H+
reduced coenzyme F0 + NADP+
-
Substrates: i.e. 7,8-didemethyl-8-hydroxy-5-deazariboflavin. The enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate
Products: -
Products: -
?
coenzyme F0 + NADPH + H+
reduced coenzyme F0 + NADP+
-
Substrates: i.e. 7,8-didemethyl-8-hydroxy-5-deazariboflavin. The enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate
Products: -
Products: -
?
coenzyme F0 + NADPH + H+
reduced coenzyme F0 + NADP+
-
Substrates: i.e. 7,8-didemethyl-8-hydroxy-5-deazariboflavin. The enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate
Products: -
Products: -
?
coenzyme F0 + NADPH + H+
reduced coenzyme F0 + NADP+
-
Substrates: i.e. 7,8-didemethyl-8-hydroxy-5-deazariboflavin. The enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate
Products: -
Products: -
?
coenzyme F0 + NADPH + H+
reduced coenzyme F0 + NADP+
-
Substrates: i.e. 7,8-didemethyl-8-hydroxy-5-deazariboflavin. The enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate
Products: -
Products: -
?
coenzyme F420 + NADPH + H+
reduced coenzyme F420 + NADP+
-
Substrates: the enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate. No activity with NAD+
Products: -
Products: -
?
coenzyme F420 + NADPH + H+
reduced coenzyme F420 + NADP+
-
Substrates: the enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate. No activity with NAD+
Products: -
Products: -
?
coenzyme F420 + NADPH + H+
reduced coenzyme F420 + NADP+
-
Substrates: the main function of this oxidoreductase is probably to provide cells with reduced 8-hydroxy-5-deazaflavin to be used in specific reduction reactions
Products: -
Products: -
?
coenzyme F420 + NADPH + H+
reduced coenzyme F420 + NADP+
-
Substrates: the enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate. No activity with NAD+
Products: -
Products: -
r
coenzyme F420 + NADPH + H+
reduced coenzyme F420 + NADP+
-
Substrates: the enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate. No activity with NAD+
Products: -
Products: -
?
coenzyme F420 + NADPH + H+
reduced coenzyme F420 + NADP+
-
Substrates: the enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate. No activity with NAD+
Products: -
Products: -
?
oxidized coenzyme F420 + NADPH + H+
reduced coenzyme F420 + NADP+
Substrates: -
Products: -
Products: -
?
oxidized coenzyme F420 + NADPH + H+
reduced coenzyme F420 + NADP+
Substrates: -
Products: -
Products: -
?
reduced coenzyme F420 + NADP+
coenzyme F420 + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
reduced coenzyme F420 + NADP+
coenzyme F420 + NADPH + H+
-
Substrates: direct hydride transfer process, A side-specific, with respect to the prochiral center C5 of the dihydro-8-hydroxy-5-deazaflavin cofactor
Products: -
Products: -
?
reduced coenzyme F420 + NADP+
coenzyme F420 + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
reduced coenzyme F420 + NADP+
coenzyme F420 + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
Substrates: -
Products: -
Products: -
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
Substrates: of the two substrates NADP+ has to bind first, the binding being associated with an induced fit. The stereochemical analysis of the hydrode transfer leads to the conclusion that the observed orientation of the Si-face of coenzyme F420 towards the Si-face of NADP+ allows only the transfer of the proS hydrogen at C5 to the proS position at C4 and vice versa
Products: -
Products: -
?
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
Substrates: the enzyme is Si face specific with respect to C5 of reduced coenzyme F420 and Si face specific with respect to C4 of NADP+. The enzyme is specific for both coenzyme F420 and NADP+/NADPH
Products: -
Products: -
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
Substrates: -
Products: -
Products: -
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
Substrates: -
Products: -
Products: -
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
Substrates: -
Products: -
Products: -
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
Substrates: -
Products: -
Products: -
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
Substrates: -
Products: -
Products: -
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
Substrates: the enzyme exhibits a sequential kinetic mechanism
Products: -
Products: -
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
Substrates: the enzyme exhibits a sequential kinetic mechanism
Products: -
Products: -
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
Substrates: -
Products: -
Products: -
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
Substrates: FNO catalyzes the NADP+ reduction more efficiently compared to NADPH oxidation
Products: -
Products: -
r
additional information
?
-
-
Substrates: F420 and the F420 redox moiety, FO, are phenolic 5-deazaflavin cofactors that complement nicotinamide and flavin redox coenzymes in biochemical oxidoreductases and photocatalytic systems. Specifically, these 5-deazaflavins lack the single electron reactivity with O2 of riboflavin-derived coenzymes (FMN and FAD), and, in general, have a more negative redox potential than NAD(P)+. A convenient synthesis of FO is achieved by improving the redox stability of synthetic intermediates containing a polar, electron-rich aminophenol fragment, Fno enzyme activity is restored with FO in the absence of F420, method optimization, overview
Products: -
Products: -
?
additional information
?
-
Substrates: effects of side chain length of residue Il135 on the donor-acceptor distance between NADP+ and the F420 precursor, FO, overview
Products: -
Products: -
?
additional information
?
-
Substrates: NADP+ binding site structure, overview. A F420-dependent enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: NADP+ binding site structure, overview. A F420-dependent enzyme
Products: -
Products: -
?
additional information
?
-
Substrates: no activity of wild-type and mutants with 1-benzylnicotinic acid
Products: -
Products: -
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
coenzyme F420 + NADPH + H+
reduced coenzyme F420 + NADP+
-
Substrates: the main function of this oxidoreductase is probably to provide cells with reduced 8-hydroxy-5-deazaflavin to be used in specific reduction reactions
Products: -
Products: -
?
reduced coenzyme F420 + NADP+
coenzyme F420 + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
reduced coenzyme F420 + NADP+
coenzyme F420 + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
reduced coenzyme F420 + NADP+
coenzyme F420 + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
Substrates: -
Products: -
Products: -
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
Substrates: -
Products: -
Products: -
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
Substrates: -
Products: -
Products: -
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
Substrates: -
Products: -
Products: -
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
Substrates: -
Products: -
Products: -
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
Substrates: -
Products: -
Products: -
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
Substrates: -
Products: -
Products: -
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
NaCl
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
the enzyme is not inhibited by iodoacetamide (20 mM), chloromercuribenzoate (20 mM) or N-ethylmaleimide (7 mM) when preincubated for 30 min in the presence of these reagents. The enzyme is not inactivated by dioxygen
-
additional information
inhibitor prediction studies reveal that lovastatin and compactin (mevastatin) produced more affinity for model structure of NADP oxidoreducatse as compared to F420. It indicates that the lovastatin and compactin (mevastatin) compounds (negative regulator) may act as potential inhibitor of F420 dependent NADP oxidoreducatse protein
-
additional information
-
inhibitor prediction studies reveal that lovastatin and compactin (mevastatin) produced more affinity for model structure of NADP oxidoreducatse as compared to F420. It indicates that the lovastatin and compactin (mevastatin) compounds (negative regulator) may act as potential inhibitor of F420 dependent NADP oxidoreducatse protein
-
additional information
inhibitor screening in a set of more than 8,000 naturally occurring small ligands and molecular docking, overview. Molecular flexibility, the number of H-bond acceptors and donors, the extent of hydrophobic interactions, and the exposure to the solvent are the major discriminants in determining the affinity of the ligands for enzyme FNO, that act in a competitive nature of the compounds of interest with NADP+ for the same site, causing a decrease in F420 reduction rates. Effects of pH and ionic strength on complex affinity
-
additional information
-
inhibitor screening in a set of more than 8,000 naturally occurring small ligands and molecular docking, overview. Molecular flexibility, the number of H-bond acceptors and donors, the extent of hydrophobic interactions, and the exposure to the solvent are the major discriminants in determining the affinity of the ligands for enzyme FNO, that act in a competitive nature of the compounds of interest with NADP+ for the same site, causing a decrease in F420 reduction rates. Effects of pH and ionic strength on complex affinity
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0155
7,8-didemethyl-8-hydroxy-5-deazariboflavin 5'-phosphate
-
pH 6.0, 22°C
2 - 3
1-hydroxyethylnicotinamide
enzyme mutant G29Y, pH 8.0, 25°C
-
0.0625
coenzyme F420
-
pH and temperature not specified in the publication
0.07
NADP+
pH 8.0, temperature not specified in the publication
0.0023
NADPH
phase I, pH 6.5, 22°C, recombinant wild-type enzyme
0.05
NADPH
pH 6.0, temperature not specified in the publication
0.062
NADPH
phase II, pH 6.5, 22°C, recombinant wild-type enzyme
0.0036
oxidized coenzyme F420
with F420 precursor, FO, pH 6.5, 22°C, recombinant mutant I135A
0.0036
oxidized coenzyme F420
with F420 precursor, FO, pH 6.5, 22°C, recombinant mutant I135G
0.0037
oxidized coenzyme F420
with F420 precursor, FO, pH 6.5, 22°C, recombinant mutant I135V
0.004
oxidized coenzyme F420
with F420 precursor, FO, pH 6.5, 22°C, recombinant wild-type enzyme
0.3
oxidized coenzyme F420
pH 6.0, temperature not specified in the publication
0.0077
reduced coenzyme F420
-
pH and temperature not specified in the publication
0.15
reduced coenzyme F420
pH 8.0, temperature not specified in the publication
additional information
additional information
steady-state kinetics
-
additional information
additional information
-
analysis of the F420 redox moiety (FO)-dependent NADP+/NADPH redox process by stopped-flow spectrophotometry, steady state kinetics, overview
-
additional information
additional information
substrate binding studies, steady-state and pre steady-state kinetic analysis with wild-type enzyme Fno and Ile135 Fno mutant variants, I135A, I135V, and I135G, overview. Steady-state kinetic analysis of wild-type Fno and the variants show classical Michaelis-Menten kinetics with varying FO concentrations. The data reveal a decreased kcat as side chain length decreased, with varying FO concentrations. The steady-state plots reveal non-Michaelis-Menten kinetic behavior when NADPH is varied. The double reciprocal plot of the varying NADPH concentrations displays a downward concave shape, while the NADPH binding curves gave Hill coefficients of less than 1. These data suggest that negative cooperativity occurs between the two identical monomers. The pre steady-state Abs420 versus time trace reveals biphasic kinetics, with a fast phase (hydride transfer) and a slow phase. The fast phase displays an increased rate constant as side chain length decreases. The rate constant for the second phase, remained about 2/s for each variant. Pre-steady-state data with F420 cofactor and NADPH for the enzyme Fno mutant variants reveal biphasic kinetics with a fast and slow phase, similar with wild-type Fno, overview
-
additional information
additional information
the enzyme shows half-site reactivity and negative cooperativity (Koshland-Nemethy-Filmer model) in the reversible reduction of NADP+ through the transfer of a hydride from the reduced F420 cofactor, steady-state kinetic analysis revealing classical Michaelis-Menten kinetics with varying concentrations of the F420 redox moiety, and non-Michaelis-Menten kinetic behavior when NADPH is varied. Pre-steady-state, stopped flow, Single-turnover, and steady-state kinetics, detailed overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE