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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
-
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
-
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
-
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
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
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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 + 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+
-
-
-
-
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+
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
-
-
-
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0.0028
1,5-dihydro-8-hydroxy-5-deazaflavin
-
pH 7.0, 20°C
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
-
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
0.04
NADP+
-
pH 8.0, 65°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
0.04
NADPH
-
pH 5.5, 65°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; pH 6.0, 25°C, recombinant mutant R51V/R55V
12
NADPH
pH 6.0, 25°C, recombinant mutant T28A/R51V; 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; above, pH 6.0, 25°C, recombinant mutant R51V
500
NADPH
above, pH 6.0, 25°C, recombinant mutant R51E/R55A; above, pH 6.0, 25°C, recombinant mutant R51E/R55N; above, pH 6.0, 25°C, recombinant mutant R51E/R55S; above, pH 6.0, 25°C, recombinant mutant R51V/R55V; above, pH 6.0, 25°C, recombinant mutant R55N; above, pH 6.0, 25°C, recombinant mutant S50E; above, pH 6.0, 25°C, recombinant mutant S50E/R55A; above, pH 6.0, 25°C, recombinant mutant S50E/R55V; above, pH 6.0, 25°C, recombinant mutant S50Q; above, pH 6.0, 25°C, recombinant mutant T28A/R51V; 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; 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

-
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
-
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
-
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7.37
1,5-dihydro-8-hydroxy-5-deazaflavin
-
pH 7.0, 20°C
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
0.11
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; 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; pH 6.0, 25°C, recombinant mutant S50E; pH 6.0, 25°C, recombinant mutant T28A/R51V
2.8
NADPH
pH 6.0, 25°C, recombinant mutant R51V/R55V; 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; pH 6.0, 25°C, recombinant mutant R55V
3.3
NADPH
pH 6.0, 25°C, recombinant mutant T28A/R51V/R55V; pH 6.0, 25°C, recombinant mutant T28A/R55A; pH 6.0, 25°C, recombinant wild-type enzyme
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
-
phase II, pH 6.5, 22°C, recombinant wild-type enzyme
5.41
NADPH
-
pH 6.5, 22°C, recombinant 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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
0.12
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 mutant R51E/R55A; pH 6.0, 25°C, recombinant wild-type enzyme
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; 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; 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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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
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
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Novotna, J.; Neuzil, J.; Hostalek, Z.
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Streptomyces griseus
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Archaeoglobus fulgidus (O29370)
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Function of coenzyme F420-dependent NADP reductase in methanogenic archaea containing an NADP-dependent alcohol dehydrogenase
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6
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Methanobrevibacter smithii (A5UJ76), Methanobrevibacter smithii, Methanobrevibacter smithii DSM 861 (A5UJ76)
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20
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Archaeoglobus fulgidus (O29370)
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438
124-126
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Methanothermobacter thermautotrophicus (D9PVP5), Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus DSM 2133 (D9PVP5)
brenda
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8-Hydroxy-5-deazaflavin-dependent electron transfer in the extreme halophile Halobacterium cutirubrum
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Halobacterium salinarum, Halobacterium salinarum NRC34001
-
brenda
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Methanococcus vannielii, Methanococcus vannielii DSM 1224
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46
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Methanosphaera stadtmanae, Methanosphaera stadtmanae DSM 3091
brenda
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Stereochemical studies of 8-hydroxy-5-deazaflavin-dependent NADP+ reductase from Methanococcus vannielii.
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Methanococcus vannielii
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Effects of isoleucine 135 side chain length on the cofactor donor-acceptor distance within F420H2NADP+ oxidoreductase A kinetic analysis
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Archaeoglobus fulgidus (O29370)
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Archaeoglobus fulgidus (O29370)
brenda
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292
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Thermobifida fusca (Q47RA9), Thermobifida fusca
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Archaea
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