1.5.1.40: 8-hydroxy-5-deazaflavin:NADPH oxidoreductase
This is an abbreviated version!
For detailed information about 8-hydroxy-5-deazaflavin:NADPH oxidoreductase, go to the full flat file.
Word Map on EC 1.5.1.40
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1.5.1.40
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methanogen
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archaea
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hydride
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8-hydroxy-5-deazaflavins
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methanococcus
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hydrogenase
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vannielii
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thermoautotrophicum
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methanobacterium
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methanobrevibacter
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griseus
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methanogenesis
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stereochemical
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smithii
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si-face
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methane
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fulgidus
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ch4
- 1.5.1.40
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methanogen
- archaea
-
hydride
- 8-hydroxy-5-deazaflavins
-
methanococcus
- hydrogenase
- vannielii
- thermoautotrophicum
-
methanobacterium
-
methanobrevibacter
- griseus
-
methanogenesis
-
stereochemical
- smithii
-
si-face
- methane
- fulgidus
- ch4
Reaction
Synonyms
5-deazaflavin-NADP+ reductase, 8-hydroxy-5-deazaflavin-dependent NADP+ reductase, 8-OH-5-deazaflavin:NADPH oxidoreductase, 8-OH-5dFl:NADPH oxidoreductase, AF0892, F420-dependent NADP oxidoreductase, F420-dependent NADP reductase, F420-dependent NADP+ oxidoreductase, F420:NADPH oxidoreductase, F420H2:NADP oxidoreductase, F420H2:NADP+ oxidoreductase, Fno, Msm_0049, NADP+:F420 oxidoreductase, Tfu-FNO, Tfu_0970
ECTree
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KM Value
KM Value on EC 1.5.1.40 - 8-hydroxy-5-deazaflavin:NADPH oxidoreductase
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0.0155
7,8-didemethyl-8-hydroxy-5-deazariboflavin 5'-phosphate
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pH 6.0, 22°C
2 - 3
enzyme mutant G29Y, pH 8.0, 25°C
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0.0625
coenzyme F420
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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
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
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pH and temperature not specified in the publication
0.15
reduced coenzyme F420
pH 8.0, temperature not specified in the publication
additional information
steady-state kinetics
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additional information
additional information
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analysis of the F420 redox moiety (FO)-dependent NADP+/NADPH redox process by stopped-flow spectrophotometry, steady state kinetics, overview
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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
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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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