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1,5-dihydro-8-hydroxy-5-deazaflavin + NADP+
8-hydroxy-5-deazaflavin + NADPH + H+
5'-O-methyl-7,8-didemethyl-8-hydroxyflavin + NADPH + H+
8-hydroxypyrimido[4,5-b]-2,4-(3H,10H)-dione + NADP+
-
the enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate
-
-
r
5-deaza-8-hydroxy-10-methylisoalloxazine + NADPH + H+
? + NADP+
5-deaza-8-hydroxyisoalloxazine + NADPH + H+
8-hydroxypyrimido[4,5-b]-2,4-(3H,10H)-dione + NADP+
-
the enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate
-
-
?
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+
-
the enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate
-
-
?
coenzyme F0 + NADPH + H+
reduced coenzyme F0 + NADP+
coenzyme F420 + NADPH + H+
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
reduced coenzyme F420 + NADP+
reduced coenzyme F420 + 1-aminoethylnicotinamide
oxidized coenzyme F420 + ?
-
-
-
?
reduced coenzyme F420 + 1-benzyl-3-acetylpyridine
oxidized coenzyme F420 + ?
-
-
-
?
reduced coenzyme F420 + 1-benzylnicotinamide
oxidized coenzyme F420 + ?
-
-
-
?
reduced coenzyme F420 + 1-ethylnicotinamide
oxidized coenzyme F420 + ?
-
-
-
?
reduced coenzyme F420 + 1-hydroxyethylnicotinamide
oxidized coenzyme F420 + ?
-
-
-
?
reduced coenzyme F420 + 1-hydroxypropylnicotinamide
oxidized coenzyme F420 + ?
-
-
-
?
reduced coenzyme F420 + 1-propylnicotinamide
oxidized coenzyme F420 + ?
-
-
-
?
reduced coenzyme F420 + NADP+
coenzyme F420 + NADPH + H+
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
additional information
?
-
1,5-dihydro-8-hydroxy-5-deazaflavin + NADP+
8-hydroxy-5-deazaflavin + NADPH + H+
-
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
-
-
r
1,5-dihydro-8-hydroxy-5-deazaflavin + NADP+
8-hydroxy-5-deazaflavin + NADPH + H+
-
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
-
-
r
5-deaza-8-hydroxy-10-methylisoalloxazine + NADPH + H+
? + NADP+
-
-
-
-
?
5-deaza-8-hydroxy-10-methylisoalloxazine + NADPH + H+
? + NADP+
-
-
-
-
?
coenzyme F0 + NADPH + H+
reduced coenzyme F0 + NADP+
-
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
-
-
?
coenzyme F0 + NADPH + H+
reduced coenzyme F0 + NADP+
-
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
-
-
?
coenzyme F0 + NADPH + H+
reduced coenzyme F0 + NADP+
-
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
-
-
?
coenzyme F0 + NADPH + H+
reduced coenzyme F0 + NADP+
-
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
-
-
?
coenzyme F0 + NADPH + H+
reduced coenzyme F0 + NADP+
-
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
-
-
?
coenzyme F420 + NADPH + H+
reduced coenzyme F420 + NADP+
-
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+
-
-
?
coenzyme F420 + NADPH + H+
reduced coenzyme F420 + NADP+
-
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+
-
-
?
coenzyme F420 + NADPH + H+
reduced coenzyme F420 + NADP+
-
the main function of this oxidoreductase is probably to provide cells with reduced 8-hydroxy-5-deazaflavin to be used in specific reduction reactions
-
-
?
coenzyme F420 + NADPH + H+
reduced coenzyme F420 + NADP+
-
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+
-
-
r
coenzyme F420 + NADPH + H+
reduced coenzyme F420 + NADP+
-
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+
-
-
?
coenzyme F420 + NADPH + H+
reduced coenzyme F420 + NADP+
-
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+
-
-
?
oxidized coenzyme F420 + NADPH + H+
reduced coenzyme F420 + NADP+
-
-
-
?
oxidized coenzyme F420 + NADPH + H+
reduced coenzyme F420 + NADP+
-
-
-
?
reduced coenzyme F420 + NADP+
coenzyme F420 + NADPH + H+
-
-
-
-
?
reduced coenzyme F420 + NADP+
coenzyme F420 + NADPH + H+
-
direct hydride transfer process, A side-specific, with respect to the prochiral center C5 of the dihydro-8-hydroxy-5-deazaflavin cofactor
-
-
?
reduced coenzyme F420 + NADP+
coenzyme F420 + NADPH + H+
-
-
-
-
r
reduced coenzyme F420 + NADP+
coenzyme F420 + NADPH + H+
-
-
-
-
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
-
-
-
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
-
-
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
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
-
-
?
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
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
-
-
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
-
-
-
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
-
-
-
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
-
-
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
-
-
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
-
-
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
-
-
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
-
-
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
-
-
-
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
-
-
-
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
-
-
-
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
-
-
-
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
the enzyme exhibits a sequential kinetic mechanism
-
-
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
the enzyme exhibits a sequential kinetic mechanism
-
-
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
-
-
-
r
reduced coenzyme F420 + NADP+
oxidized coenzyme F420 + NADPH + H+
FNO catalyzes the NADP+ reduction more efficiently compared to NADPH oxidation
-
-
r
additional information
?
-
-
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
-
-
?
additional information
?
-
effects of side chain length of residue Il135 on the donor-acceptor distance between NADP+ and the F420 precursor, FO, overview
-
-
?
additional information
?
-
NADP+ binding site structure, overview. A F420-dependent enzyme
-
-
?
additional information
?
-
-
NADP+ binding site structure, overview. A F420-dependent enzyme
-
-
?
additional information
?
-
no activity of wild-type and mutants with 1-benzylnicotinic acid
-
-
-
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0.0028
1,5-dihydro-8-hydroxy-5-deazaflavin
-
pH 7.0, 20°C
2 - 18
1-aminoethylnicotinamide
-
7.4
1-benzyl-3-acetylpyridine
wild-type enzyme, pH 8.0, 25°C
-
4.3 - 9.5
1-benzylnicotinamide
-
25
1-ethylnicotinamide
wild-type enzyme, pH 8.0, 25°C
-
2 - 33
1-hydroxyethylnicotinamide
-
25 - 35
1-hydroxypropylnicotinamide
-
5.7 - 35
1-propylnicotinamide
-
0.0135
5'-O-methyl-7,8-didemethyl-8-hydroxyflavin
-
pH 6.0, 22°C
0.0193
5-deaza-8-hydroxyisoalloxazine
-
pH 6.0, 22°C
0.0155
7,8-didemethyl-8-hydroxy-5-deazariboflavin 5'-phosphate
-
pH 6.0, 22°C
0.008
8-hydroxy-5-deazaflavin
-
pH 7.0, 20°C
0.0775
8-hydroxypyrimido[4,5-b]-2,4-(3H,10H)-dione
-
pH 6.0, 22°C
0.0057
coenzyme F0
-
pH 6.0, 22°C
0.0034 - 0.0625
coenzyme F420
0.0036 - 4
oxidized coenzyme F420
0.0077 - 0.15
reduced coenzyme F420
additional information
additional information
-
2 - 3
1-aminoethylnicotinamide
enzyme mutant G29Y, pH 8.0, 25°C
-
12
1-aminoethylnicotinamide
wild-type enzyme, pH 8.0, 25°C
-
14
1-aminoethylnicotinamide
enzyme mutant P98H, pH 8.0, 25°C
-
18
1-aminoethylnicotinamide
enzyme mutant G29S, pH 8.0, 25°C
-
4.3
1-benzylnicotinamide
enzyme mutant G29W, pH 8.0, 25°C
-
6.4
1-benzylnicotinamide
wild-type enzyme, pH 8.0, 25°C
-
9.5
1-benzylnicotinamide
enzyme mutant G29Y, pH 8.0, 25°C
-
2 - 3
1-hydroxyethylnicotinamide
enzyme mutant G29Y, pH 8.0, 25°C
-
20
1-hydroxyethylnicotinamide
wild-type enzyme, pH 8.0, 25°C
-
20
1-hydroxyethylnicotinamide
enzyme mutant P98H, pH 8.0, 25°C
-
33
1-hydroxyethylnicotinamide
enzyme mutant P98Y, pH 8.0, 25°C
-
25
1-hydroxypropylnicotinamide
wild-type enzyme, pH 8.0, 25°C
-
35
1-hydroxypropylnicotinamide
enzyme mutant P89Y, pH 8.0, 25°C
-
5.7
1-propylnicotinamide
enzyme mutant P89H, pH 8.0, 25°C
-
10
1-propylnicotinamide
wild-type enzyme, pH 8.0, 25°C
-
18
1-propylnicotinamide
enzyme mutant G29L, pH 8.0, 25°C
-
27
1-propylnicotinamide
enzyme mutant P89L, pH 8.0, 25°C
-
35
1-propylnicotinamide
enzyme mutant P89Y, pH 8.0, 25°C
-
0.0034
coenzyme F420
-
pH 6.0, 22°C
0.0625
coenzyme F420
-
pH and temperature not specified in the publication
0.0137
NADP+
-
pH 7.0, 20°C
0.0144
NADP+
-
pH 6.0, 22°C
0.07
NADP+
pH 8.0, temperature not specified in the publication
0.37
NADP+
-
pH and temperature not specified in the publication
0.00027
NADPH
phase I, pH 6.5, 22°C, recombinant mutant I135A
0.0007
NADPH
phase I, pH 6.5, 22°C, recombinant mutant I135V
0.0023
NADPH
phase I, pH 6.5, 22°C, recombinant wild-type enzyme
0.0029
NADPH
phase II, pH 6.5, 22°C, recombinant mutant I135A
0.0104
NADPH
-
pH 7.0, 20°C
0.016
NADPH
phase I, pH 6.5, 22°C, recombinant mutant I135G
0.0195
NADPH
-
pH 6.0, 22°C
0.05
NADPH
pH 6.0, temperature not specified in the publication
0.051
NADPH
phase II, pH 6.5, 22°C, recombinant mutant I135V
0.062
NADPH
phase II, pH 6.5, 22°C, recombinant wild-type enzyme
0.142
NADPH
-
pH and temperature not specified in the publication
0.654
NADPH
phase II, pH 6.5, 22°C, recombinant mutant I135G
3.2
NADPH
pH 6.0, 25°C, recombinant mutant S50E
4.4
NADPH
pH 6.0, 25°C, recombinant mutant R55S
5
NADPH
pH 6.0, 25°C, recombinant mutant T28A
5.4
NADPH
pH 6.0, 25°C, recombinant mutant T28A/R55A
6.3
NADPH
pH 6.0, 25°C, recombinant mutant R55N
6.5
NADPH
pH 6.0, 25°C, recombinant mutant R51E/R55N
7
NADPH
pH 6.0, 25°C, recombinant mutant R55A
7.3
NADPH
pH 6.0, 25°C, recombinant wild-type enzyme
8.2
NADPH
pH 6.0, 25°C, recombinant mutant S50Q
8.6
NADPH
pH 6.0, 25°C, recombinant mutant R51A
8.7
NADPH
pH 6.0, 25°C, recombinant mutant R51V
9.6
NADPH
pH 6.0, 25°C, recombinant mutant R55V
9.8
NADPH
pH 6.0, 25°C, recombinant mutant S50E/R55V
10
NADPH
pH 6.0, 25°C, recombinant mutant R51E/R55A
10
NADPH
pH 6.0, 25°C, recombinant mutant R51V/R55V
12
NADPH
pH 6.0, 25°C, recombinant mutant T28A/R51V
12
NADPH
pH 6.0, 25°C, recombinant mutant T28A/R51V/R55V
14
NADPH
pH 6.0, 25°C, recombinant wild-type enzyme
19
NADPH
pH 6.0, 25°C, recombinant mutant T28A
20
NADPH
pH 6.0, 25°C, recombinant mutant S50E/R55A
29
NADPH
pH 6.0, 25°C, recombinant mutant R55A
32
NADPH
pH 6.0, 25°C, recombinant mutant R51E/R55S
49
NADPH
pH 6.0, 25°C, recombinant mutant R55V
61.6
NADPH
pH 6.5, 22°C, recombinant enzyme
93
NADPH
pH 6.0, 25°C, recombinant mutant T28A/R55A
170
NADPH
pH 6.0, 25°C, recombinant mutant R55S
180
NADPH
above, pH 6.0, 25°C, recombinant mutant R51A
180
NADPH
above, pH 6.0, 25°C, recombinant mutant R51V
500
NADPH
above, pH 6.0, 25°C, recombinant mutant R51E/R55A
500
NADPH
above, pH 6.0, 25°C, recombinant mutant R51E/R55N
500
NADPH
above, pH 6.0, 25°C, recombinant mutant R51E/R55S
500
NADPH
above, pH 6.0, 25°C, recombinant mutant R51V/R55V
500
NADPH
above, pH 6.0, 25°C, recombinant mutant R55N
500
NADPH
above, pH 6.0, 25°C, recombinant mutant S50E
500
NADPH
above, pH 6.0, 25°C, recombinant mutant S50E/R55A
500
NADPH
above, pH 6.0, 25°C, recombinant mutant S50E/R55V
500
NADPH
above, pH 6.0, 25°C, recombinant mutant S50Q
500
NADPH
above, pH 6.0, 25°C, recombinant mutant T28A/R51V
500
NADPH
above, pH 6.0, 25°C, recombinant mutant T28A/R51V/R55V
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
0.01
oxidized coenzyme F420
pH 5.5, 65°C
0.1
oxidized coenzyme F420
pH 6.0, 30°C
0.3
oxidized coenzyme F420
pH 6.0, temperature not specified in the publication
2
oxidized coenzyme F420
pH 6.0, 25°C, recombinant enzyme
4
oxidized coenzyme F420
pH 6.5, 22°C, recombinant enzyme
0.0077
reduced coenzyme F420
-
pH and temperature not specified in the publication
0.0129
reduced coenzyme F420
-
pH 6.0, 22°C
0.02
reduced coenzyme F420
pH 8.0, 65°C
0.04
reduced coenzyme F420
pH 8.0, 30°C
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
7.37
1,5-dihydro-8-hydroxy-5-deazaflavin
-
pH 7.0, 20°C
0.0233 - 0.16
1-aminoethylnicotinamide
-
0.0042
1-benzyl-3-acetylpyridine
wild-type enzyme, pH 8.0, 25°C
-
0.0045 - 0.417
1-benzylnicotinamide
-
0.0073
1-ethylnicotinamide
wild-type enzyme, pH 8.0, 25°C
-
0.0233 - 0.103
1-hydroxyethylnicotinamide
-
0.0042 - 0.0118
1-hydroxypropylnicotinamide
-
0.0015 - 0.0098
1-propylnicotinamide
-
6.5
5'-O-methyl-7,8-didemethyl-8-hydroxyflavin
-
pH 6.0, 22°C
4.4
5-deaza-8-hydroxyisoalloxazine
-
pH 6.0, 22°C
35.57
7,8-didemethyl-8-hydroxy-5-deazariboflavin 5'-phosphate
-
pH 6.0, 22°C
175
8-hydroxy-5-deazaflavin
-
pH 7.0, 20°C
10.23
8-hydroxypyrimido[4,5-b]-2,4-(3H,10H)-dione
-
pH 6.0, 22°C
12.15
coenzyme F0
-
pH 6.0, 22°C
17.22
coenzyme F420
-
pH 6.0, 22°C
7.37
NADP+
-
pH 7.0, 20°C
0.7 - 5.3
oxidized coenzyme F420
3
reduced coenzyme F420
-
pH 6.0, 22°C
0.0233
1-aminoethylnicotinamide
wild-type enzyme, pH 8.0, 25°C
-
0.042
1-aminoethylnicotinamide
enzyme mutant P98H, pH 8.0, 25°C
-
0.053
1-aminoethylnicotinamide
enzyme mutant G29Y, pH 8.0, 25°C
-
0.16
1-aminoethylnicotinamide
enzyme mutant G29S, pH 8.0, 25°C
-
0.0045
1-benzylnicotinamide
wild-type enzyme, pH 8.0, 25°C
-
0.145
1-benzylnicotinamide
enzyme mutant G29Y, pH 8.0, 25°C
-
0.417
1-benzylnicotinamide
enzyme mutant G29W, pH 8.0, 25°C
-
0.0233
1-hydroxyethylnicotinamide
wild-type enzyme, pH 8.0, 25°C
-
0.048
1-hydroxyethylnicotinamide
enzyme mutant P98H, pH 8.0, 25°C
-
0.083
1-hydroxyethylnicotinamide
enzyme mutant P98Y, pH 8.0, 25°C
-
0.103
1-hydroxyethylnicotinamide
enzyme mutant G29Y, pH 8.0, 25°C
-
0.0042
1-hydroxypropylnicotinamide
wild-type enzyme, pH 8.0, 25°C
-
0.0118
1-hydroxypropylnicotinamide
enzyme mutant P89Y, pH 8.0, 25°C
-
0.0015
1-propylnicotinamide
wild-type enzyme, pH 8.0, 25°C
-
0.0045
1-propylnicotinamide
enzyme mutant P89H, pH 8.0, 25°C
-
0.006
1-propylnicotinamide
enzyme mutant G29L, pH 8.0, 25°C
-
0.0073
1-propylnicotinamide
enzyme mutant P89L, pH 8.0, 25°C
-
0.0098
1-propylnicotinamide
enzyme mutant P89Y, pH 8.0, 25°C
-
0.11
NADPH
phase I, pH 6.5, 22°C, recombinant mutant I135G
0.33
NADPH
phase II, pH 6.5, 22°C, recombinant mutant I135G
0.91
NADPH
phase I, pH 6.5, 22°C, recombinant mutant I135A
1.24
NADPH
phase II, pH 6.5, 22°C, recombinant mutant I135A
1.3
NADPH
above, pH 6.0, 25°C, recombinant mutant R51V
1.5
NADPH
phase I, pH 6.5, 22°C, recombinant mutant I135V
1.6
NADPH
above, pH 6.0, 25°C, recombinant mutant R51A
1.6
NADPH
pH 6.0, 25°C, recombinant mutant R51E/R55A
1.8
NADPH
pH 6.0, 25°C, recombinant mutant S50E/R55V
2.16
NADPH
phase II, pH 6.5, 22°C, recombinant mutant I135V
2.2
NADPH
pH 6.0, 25°C, recombinant wild-type enzyme
2.3
NADPH
pH 6.0, 25°C, recombinant mutant S50E/R55A
2.5
NADPH
pH 6.0, 25°C, recombinant mutant T28A/R55A
2.6
NADPH
pH 6.0, 25°C, recombinant mutant T28A
2.7
NADPH
pH 6.0, 25°C, recombinant mutant R51E/R55N
2.7
NADPH
pH 6.0, 25°C, recombinant mutant S50E
2.7
NADPH
pH 6.0, 25°C, recombinant mutant T28A/R51V
2.8
NADPH
pH 6.0, 25°C, recombinant mutant R51V/R55V
2.8
NADPH
pH 6.0, 25°C, recombinant mutant R55N
3
NADPH
pH 6.0, 25°C, recombinant mutant R55A
3.2
NADPH
pH 6.0, 25°C, recombinant mutant R51A
3.2
NADPH
pH 6.0, 25°C, recombinant mutant R55V
3.3
NADPH
pH 6.0, 25°C, recombinant wild-type enzyme
3.3
NADPH
pH 6.0, 25°C, recombinant mutant T28A/R51V/R55V
3.3
NADPH
pH 6.0, 25°C, recombinant mutant T28A/R55A
3.4
NADPH
pH 6.0, 25°C, recombinant mutant R51V
3.5
NADPH
pH 6.0, 25°C, recombinant mutant R55S
4.16
NADPH
phase I, pH 6.5, 22°C, recombinant wild-type enzyme
4.2
NADPH
pH 6.0, 25°C, recombinant mutant S50Q
4.9
NADPH
pH 6.0, 25°C, recombinant mutant R51E/R55S
5.41
NADPH
pH 6.5, 22°C, recombinant enzyme
5.41
NADPH
phase II, pH 6.5, 22°C, recombinant wild-type enzyme
6.9
NADPH
pH 6.0, 25°C, recombinant mutant R55S
8.8
NADPH
pH 6.0, 25°C, recombinant mutant R55A
14
NADPH
pH 6.0, 25°C, recombinant mutant T28A
0.7
oxidized coenzyme F420
with F420 precursor, FO, pH 6.5, 22°C, recombinant mutant I135G
1.6
oxidized coenzyme F420
with F420 precursor, FO, pH 6.5, 22°C, recombinant mutant I135A
1.8
oxidized coenzyme F420
with F420 precursor, FO, pH 6.5, 22°C, recombinant mutant I135V
5.27
oxidized coenzyme F420
pH 6.5, 22°C, recombinant enzyme
5.3
oxidized coenzyme F420
with F420 precursor, FO, pH 6.5, 22°C, recombinant wild-type enzyme
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0.00194 - 0.0088
1-aminoethylnicotinamide
-
0.00057
1-benzyl-3-acetylpyridine
wild-type enzyme, pH 8.0, 25°C
-
0.0007 - 0.097
1-benzylnicotinamide
-
0.00029
1-ethylnicotinamide
wild-type enzyme, pH 8.0, 25°C
-
0.0012 - 0.0045
1-hydroxyethylnicotinamide
-
0.00017 - 0.00034
1-hydroxypropylnicotinamide
-
0.00015 - 0.00079
1-propylnicotinamide
-
48
5'-O-methyl-7,8-didemethyl-8-hydroxyflavin
-
pH 6.0, 22°C
23
5-deaza-8-hydroxyisoalloxazine
-
pH 6.0, 22°C
2295
7,8-didemethyl-8-hydroxy-5-deazariboflavin 5'-phosphate
-
pH 6.0, 22°C
132
8-hydroxypyrimido[4,5-b]-2,4-(3H,10H)-dione
-
pH 6.0, 22°C
2132
coenzyme F0
-
pH 6.0, 22°C
5065
coenzyme F420
-
pH 6.0, 22°C
194.4 - 1325
oxidized coenzyme F420
233
reduced coenzyme F420
-
pH 6.0, 22°C
0.00194
1-aminoethylnicotinamide
wild-type enzyme, pH 8.0, 25°C
-
0.0023
1-aminoethylnicotinamide
enzyme mutant G29Y, pH 8.0, 25°C
-
0.003
1-aminoethylnicotinamide
enzyme mutant P98H, pH 8.0, 25°C
-
0.0088
1-aminoethylnicotinamide
enzyme mutant G29S, pH 8.0, 25°C
-
0.0007
1-benzylnicotinamide
wild-type enzyme, pH 8.0, 25°C
-
0.0153
1-benzylnicotinamide
enzyme mutant G29Y, pH 8.0, 25°C
-
0.097
1-benzylnicotinamide
enzyme mutant G29W, pH 8.0, 25°C
-
0.0012
1-hydroxyethylnicotinamide
wild-type enzyme, pH 8.0, 25°C
-
0.0024
1-hydroxyethylnicotinamide
enzyme mutant P98H, pH 8.0, 25°C
-
0.0025
1-hydroxyethylnicotinamide
enzyme mutant P98Y, pH 8.0, 25°C
-
0.0045
1-hydroxyethylnicotinamide
enzyme mutant G29Y, pH 8.0, 25°C
-
0.00017
1-hydroxypropylnicotinamide
wild-type enzyme, pH 8.0, 25°C
-
0.00034
1-hydroxypropylnicotinamide
enzyme mutant P89Y, pH 8.0, 25°C
-
0.00015
1-propylnicotinamide
wild-type enzyme, pH 8.0, 25°C
-
0.00027
1-propylnicotinamide
enzyme mutant P89L, pH 8.0, 25°C
-
0.00028
1-propylnicotinamide
enzyme mutant P89Y, pH 8.0, 25°C
-
0.00033
1-propylnicotinamide
enzyme mutant G29L, pH 8.0, 25°C
-
0.00079
1-propylnicotinamide
enzyme mutant P89H, pH 8.0, 25°C
-
0.12
NADPH
pH 6.0, 25°C, recombinant mutant S50E/R55A
0.15
NADPH
pH 6.0, 25°C, recombinant mutant R51E/R55S
0.16
NADPH
pH 6.0, 25°C, recombinant wild-type enzyme
0.16
NADPH
pH 6.0, 25°C, recombinant mutant R51E/R55A
0.18
NADPH
pH 6.0, 25°C, recombinant mutant S50E/R55V
0.23
NADPH
pH 6.0, 25°C, recombinant mutant T28A/R51V
0.28
NADPH
pH 6.0, 25°C, recombinant mutant R51V/R55V
0.28
NADPH
pH 6.0, 25°C, recombinant mutant T28A/R51V/R55V
0.29
NADPH
pH 6.0, 25°C, recombinant mutant R51V
0.33
NADPH
pH 6.0, 25°C, recombinant mutant R55V
0.37
NADPH
pH 6.0, 25°C, recombinant mutant R51A
0.42
NADPH
pH 6.0, 25°C, recombinant mutant R51E/R55N
0.42
NADPH
pH 6.0, 25°C, recombinant mutant R55A
0.44
NADPH
pH 6.0, 25°C, recombinant mutant R55N
0.46
NADPH
pH 6.0, 25°C, recombinant mutant T28A/R55A
0.5
NADPH
phase II, pH 6.5, 22°C, recombinant mutant I135G
0.51
NADPH
pH 6.0, 25°C, recombinant mutant S50Q
0.52
NADPH
pH 6.0, 25°C, recombinant mutant T28A
0.79
NADPH
pH 6.0, 25°C, recombinant mutant R55S
0.84
NADPH
pH 6.0, 25°C, recombinant mutant S50E
3.5
NADPH
pH 6.0, 25°C, recombinant mutant T28A/R55A
6.2
NADPH
above, pH 6.0, 25°C, recombinant mutant R51A
6.8
NADPH
phase I, pH 6.5, 22°C, recombinant mutant I135G
9.3
NADPH
above, pH 6.0, 25°C, recombinant mutant R51V
41
NADPH
pH 6.0, 25°C, recombinant mutant R55S
42
NADPH
phase II, pH 6.5, 22°C, recombinant mutant I135V
88
NADPH
phase II, pH 6.5, 22°C, recombinant wild-type enzyme
300
NADPH
pH 6.0, 25°C, recombinant mutant R55A
420
NADPH
phase II, pH 6.5, 22°C, recombinant mutant I135A
450
NADPH
pH 6.0, 25°C, recombinant wild-type enzyme
720
NADPH
pH 6.0, 25°C, recombinant mutant T28A
1800
NADPH
phase I, pH 6.5, 22°C, recombinant wild-type enzyme
2100
NADPH
phase I, pH 6.5, 22°C, recombinant mutant I135V
3400
NADPH
phase I, pH 6.5, 22°C, recombinant mutant I135A
194.4
oxidized coenzyme F420
with F420 precursor, FO, pH 6.5, 22°C, recombinant mutant I135G
444.4
oxidized coenzyme F420
with F420 precursor, FO, pH 6.5, 22°C, recombinant mutant I135A
486.5
oxidized coenzyme F420
with F420 precursor, FO, pH 6.5, 22°C, recombinant mutant I135V
1325
oxidized coenzyme F420
with F420 precursor, FO, pH 6.5, 22°C, recombinant wild-type enzyme
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malfunction
T28A mutant shows 3fold increased kinetic efficiency compared with the wild-type enzyme when NADPH is the substrate
physiological function
-
the main function of this oxidoreductase is probably to provide cells with reduced 8-hydroxy-5-deazaflavin to be used in specific reduction reactions. The last step of the tetracycline biosynthesis in Streptomyces aureofaciens in which 5a,11a-dehydrochlortetracycline is reduced to chlortetracycline is 8-hydroxy-5-deazaflavin-dependent, and the reducing equivalents are obtained from NADPH
physiological function
-
F420-dependent NADP+ oxidoreductase (Fno) is critical to the conversion of CO2 to CH4 by methanogenic archaea, while the F420 redox moiety, FO, functions as a light-harvesting agent in DNA repair
physiological function
half-site reactivity and negative cooperativity involving the important F420 cofactor-dependent enzyme. F420H2:NADP+ oxidoreductase (Fno), an F420 cofactor-dependent enzyme that catalyzes the reversible reduction of NADP+ through the transfer of a hydride from the reduced F420 cofactor. Fno may be a functional regulatory enzyme
physiological function
residue I135 plays a key role in sustaining the donor-acceptor distance between the two cofactor substrates, thereby regulating the rate at which the hydride is transferred from FOH2 to NADP+. Fno is a dynamic enzyme that regulates NADPH production
physiological function
the enzyme catalyses the bidirectional electron transfer between NADP+ and F420H2 during the intestinal production of CH4 from CO2
physiological function
-
the enzyme catalyses the bidirectional electron transfer between NADP+ and F420H2 during the intestinal production of CH4 from CO2
-
physiological function
-
the enzyme catalyses the bidirectional electron transfer between NADP+ and F420H2 during the intestinal production of CH4 from CO2
-
physiological function
-
the enzyme catalyses the bidirectional electron transfer between NADP+ and F420H2 during the intestinal production of CH4 from CO2
-
physiological function
-
the enzyme catalyses the bidirectional electron transfer between NADP+ and F420H2 during the intestinal production of CH4 from CO2
-
additional information
the active site of F420-dependent enzyme Tfu-FNO is located in a hydrophobic pocket between an N-terminal dinucleotide binding domain and a smaller C-terminal domain. Residues interacting with the 2'-phosphate of NADP+, Thr28, Ser50, Arg51, and Arg55, are important for discriminating between NADP+ and NAD+. Molecular recognition of the two cofactor substrates, F420 and NAD(P)H by FNO, overview
additional information
-
the active site of F420-dependent enzyme Tfu-FNO is located in a hydrophobic pocket between an N-terminal dinucleotide binding domain and a smaller C-terminal domain. Residues interacting with the 2'-phosphate of NADP+, Thr28, Ser50, Arg51, and Arg55, are important for discriminating between NADP+ and NAD+. Molecular recognition of the two cofactor substrates, F420 and NAD(P)H by FNO, overview
additional information
FNO from Methanobrevibacter smithii is homology-modelled using the 3D structure FNO from Archaeoglobus fulgidus as template. The computationally validated predictive model consists of a major globular core, with 44% helices (41% alpha-helices, 3% 3(10)-helices), 22% beta-sheets content, and extensive polar surfaces, catalytic site structure revealing a negatively polarized narrow pocket surrounded by positively polarized surfaces, this opposite polarity being among the pivotal factors determining the selectivity for both substrate and (most likely) site-directed ligands/inhibitors, molecular docking, detailed overview
additional information
-
FNO from Methanobrevibacter smithii is homology-modelled using the 3D structure FNO from Archaeoglobus fulgidus as template. The computationally validated predictive model consists of a major globular core, with 44% helices (41% alpha-helices, 3% 3(10)-helices), 22% beta-sheets content, and extensive polar surfaces, catalytic site structure revealing a negatively polarized narrow pocket surrounded by positively polarized surfaces, this opposite polarity being among the pivotal factors determining the selectivity for both substrate and (most likely) site-directed ligands/inhibitors, molecular docking, detailed overview
additional information
-
FNO from Methanobrevibacter smithii is homology-modelled using the 3D structure FNO from Archaeoglobus fulgidus as template. The computationally validated predictive model consists of a major globular core, with 44% helices (41% alpha-helices, 3% 3(10)-helices), 22% beta-sheets content, and extensive polar surfaces, catalytic site structure revealing a negatively polarized narrow pocket surrounded by positively polarized surfaces, this opposite polarity being among the pivotal factors determining the selectivity for both substrate and (most likely) site-directed ligands/inhibitors, molecular docking, detailed overview
-
additional information
-
FNO from Methanobrevibacter smithii is homology-modelled using the 3D structure FNO from Archaeoglobus fulgidus as template. The computationally validated predictive model consists of a major globular core, with 44% helices (41% alpha-helices, 3% 3(10)-helices), 22% beta-sheets content, and extensive polar surfaces, catalytic site structure revealing a negatively polarized narrow pocket surrounded by positively polarized surfaces, this opposite polarity being among the pivotal factors determining the selectivity for both substrate and (most likely) site-directed ligands/inhibitors, molecular docking, detailed overview
-
additional information
-
FNO from Methanobrevibacter smithii is homology-modelled using the 3D structure FNO from Archaeoglobus fulgidus as template. The computationally validated predictive model consists of a major globular core, with 44% helices (41% alpha-helices, 3% 3(10)-helices), 22% beta-sheets content, and extensive polar surfaces, catalytic site structure revealing a negatively polarized narrow pocket surrounded by positively polarized surfaces, this opposite polarity being among the pivotal factors determining the selectivity for both substrate and (most likely) site-directed ligands/inhibitors, molecular docking, detailed overview
-
additional information
-
FNO from Methanobrevibacter smithii is homology-modelled using the 3D structure FNO from Archaeoglobus fulgidus as template. The computationally validated predictive model consists of a major globular core, with 44% helices (41% alpha-helices, 3% 3(10)-helices), 22% beta-sheets content, and extensive polar surfaces, catalytic site structure revealing a negatively polarized narrow pocket surrounded by positively polarized surfaces, this opposite polarity being among the pivotal factors determining the selectivity for both substrate and (most likely) site-directed ligands/inhibitors, molecular docking, detailed overview
-
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I135A
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
I135G
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
I135V
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
G29L
site-directed mutagenesis, the mutant shows altered kinetics and increased catalytic efficiency with nicotinamide cofactor biomimetics compared to wild-type enzyme
G29S
site-directed mutagenesis, the mutant shows altered kinetics and increased catalytic efficiency with nicotinamide cofactor biomimetics compared to wild-type enzyme
G29Y
site-directed mutagenesis, the mutant shows altered kinetics and increased catalytic efficiency with nicotinamide cofactor biomimetics compared to wild-type enzyme
P89H
site-directed mutagenesis, the mutant shows altered kinetics and increased catalytic efficiency with nicotinamide cofactor biomimetics compared to wild-type enzyme
P89L
site-directed mutagenesis, the mutant shows altered kinetics and increased catalytic efficiency with nicotinamide cofactor biomimetics compared to wild-type enzyme
P89Y
site-directed mutagenesis, the mutant shows altered kinetics and increased catalytic efficiency with nicotinamide cofactor biomimetics compared to wild-type enzyme
R51A
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type enzyme
R51E/R55A
site-directed mutagenesis, the mutant shows similar catalytic efficiency compared to the wild-type enzyme
R51E/R55N
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type enzyme
R51E/R55S
site-directed mutagenesis, the mutant shows similar catalytic efficiency compared to the wild-type enzyme
R51V
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type enzyme
R51V/R55V
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type enzyme
R55A
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type enzyme
R55N
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type enzyme
R55S
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type enzyme
R55V
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type enzyme
S50E
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type enzyme
S50E/R55A
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
S50E/R55V
site-directed mutagenesis, the mutant shows slightly increased catalytic efficiency compared to the wild-type enzyme
S50Q
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type enzyme
T28A
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type enzyme
T28A/R51V
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type enzyme
T28A/R51V/R55V
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type enzyme
T28A/R55A
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type enzyme
additional information
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
engineering of the thermostable F420:NADPH oxidoreductase from Thermobifida fusca (Tfu-FNO) by structure-inspired site-directed mutagenesis to accommodate the unnatural N1 substituents of eight nicotinamide cofactor biomimetics (NCBs). The extraordinarily low redox potential of the natural cofactor F420H2 is then exploited to reduce these NCBs. Wild-type enzyme has detectable activity toward all selected NCBs. Saturation mutagenesis at positions Gly29 and Pro89 results in mutants with up to 139times higher catalytic efficiencies, kinetics comparisons, overview. Most mutations significantly decrease the activity toward NADP+ but do not completely inhibit the enzyme for this cosubstrate
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Novotna, J.; Neuzil, J.; Hostalek, Z.
Spectrophotometric identification of 8-hydroxy-5-deazaflavin. NADPH oxidoreductase activity in Streptomyces producing tetracyclines
FEMS Microbiol. Lett.
59
241-246
1989
Kitasatospora aureofaciens, Streptomyces rimosus, Streptomyces rimosus P, Kitasatospora aureofaciens 84/25
-
brenda
Eker, A.P.; Hessels, J.K.; Meerwaldt, R.
Characterization of an 8-hydroxy-5-deazaflavin:NADPH oxidoreductase from Streptomyces griseus
Biochim. Biophys. Acta
990
80-86
1989
Streptomyces griseus
brenda
Kunow,J.; Schwrer, B.; Stetter, K.O.; Thauer, R.K.
A F420-dependent NADP reductase in the extremely thermophilie sulfate-reducing Archaeoglobus fulgidus
Arch. Microbiol.
160
199-205
1993
Archaeoglobus fulgidus (O29370)
-
brenda
Berk, H.; Thauer, R.K.
Function of coenzyme F420-dependent NADP reductase in methanogenic archaea containing an NADP-dependent alcohol dehydrogenase
Arch. Microbiol.
168
396-402
1997
Methanobacterium palustre, Methanofollis liminatans, Methanoculleus thermophilus, Methanogenium organophilum (P80951), Methanogenium organophilum, Methanofollis liminatans DSM 4140, Methanogenium organophilum DSM 3596 (P80951), Methanobacterium palustre DSM 3108, Methanoculleus thermophilus DSM 3915
brenda
Sharma, A.; Chaudhary, P.P.; Sirohi, S.K.; Saxena, J.
Structure modeling and inhibitor prediction ofNADP oxidoreductase enzyme from Methanobrevibacter smithii
Bioinformation
6
15-19
2011
Methanobrevibacter smithii (A5UJ76), Methanobrevibacter smithii, Methanobrevibacter smithii DSM 861 (A5UJ76)
brenda
Warkentin, E.; Mamat, B.; Sordel-Klippert, M.; Wicke, M.; Thauer, R.K.; Iwata, M.; Iwata, S.; Ermler, U.; Shima, S.
Structures of F420H2:NADP+ oxidoreductase with and without its substrates bound
EMBO J.
20
6561-6569
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Archaeoglobus fulgidus (O29370)
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Berk, H.; Thauer, R.K.
F420H2:NADP oxidoreductase from Methanobacterium thermoautotrophicum: identification of the encoding gene via functional overexpression in Escherichia coli
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438
124-126
1998
Methanothermobacter thermautotrophicus (D9PVP5), Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus DSM 2133 (D9PVP5)
brenda
de Wott, L.E.A.; Eker, A.P.M.
8-Hydroxy-5-deazaflavin-dependent electron transfer in the extreme halophile Halobacterium cutirubrum
FEMS Microbiol. Lett.
48(1-2)
121-125
1987
Halobacterium salinarum, Halobacterium salinarum NRC34001
-
brenda
Yamazaki, S.; Tsai, L.
Purification and properties of 8-hydroxy-5-deazaflavin-dependent NADP+ reductase from Methanococcus vannielii
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255
6462-6465
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Methanococcus vannielii, Methanococcus vannielii DSM 1224
brenda
Elias, D.A.; Juck, D.F.; Berry, K.A.; Sparling, R.
Purification of the NADP+:F420 oxidoreductase of Methanosphaera stadtmanae
Can. J. Microbiol.
46
998-1003
2000
Methanosphaera stadtmanae, Methanosphaera stadtmanae DSM 3091
brenda
Yamazaki, S.; Tsai, L.; Stadtman, T.C.; Jacobson, F.S.; Walsh, C.
Stereochemical studies of 8-hydroxy-5-deazaflavin-dependent NADP+ reductase from Methanococcus vannielii.
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Effects of isoleucine 135 side chain length on the cofactor donor-acceptor distance within F420H2 NADP+ oxidoreductase A kinetic analysis
Biochem. Biophys. Rep.
9
114-120
2017
Archaeoglobus fulgidus (O29370)
brenda
Joseph, E.; Le, C.Q.; Nguyen, T.; Oyugi, M.; Hossain, M.S.; Foss, F.W.; Johnson-Winters, K.
Evidence of negative cooperativity and half-site reactivity within an F420-dependent enzyme kinetic analysis of F420H2 NADP+ oxidoreductase
Biochemistry
55
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Archaeoglobus fulgidus (O29370)
brenda
Kumar, H.; Nguyen, Q.T.; Binda, C.; Mattevi, A.; Fraaije, M.W.
Isolation and characterization of a thermostable F420 NADPH oxidoreductase from Thermobifida fusca
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292
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brenda
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Convenient synthesis of deazaflavin cofactor FO and its activity in F420-dependent NADP reductase
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Drenth, J.; Yang, G.; Paul, C.E.; Fraaije, M.W.
A tailor-made deazaflavin-mediated recycling system for artificial nicotinamide cofactor biomimetics
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11
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Thermobifida fusca (Q47RA9)
brenda
Cuccioloni, M.; Bonfili, L.; Cecarini, V.; Cocchioni, F.; Petrelli, D.; Crotti, E.; Zanchi, R.; Eleuteri, A.M.; Angeletti, M.
Structure/activity virtual screening and in vitro testing of small molecule inhibitors of 8-hydroxy-5-deazaflavin NADPH oxidoreductase from gut methanogenic bacteria
Sci. Rep.
10
13150
2020
Methanobrevibacter smithii (A5UJ76), Methanobrevibacter smithii, Methanobrevibacter smithii DSM 861 (A5UJ76), Methanobrevibacter smithii OCM 144 (A5UJ76), Methanobrevibacter smithii PS (A5UJ76), Methanobrevibacter smithii ATCC 35061 (A5UJ76)
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