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
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methanococcus
- hydrogenase
- vannielii
- thermoautotrophicum
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methanobacterium
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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
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General Information
General Information on EC 1.5.1.40 - 8-hydroxy-5-deazaflavin:NADPH oxidoreductase
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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
additional information
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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
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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
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the enzyme catalyses the bidirectional electron transfer between NADP+ and F420H2 during the intestinal production of CH4 from CO2
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physiological function
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the enzyme catalyses the bidirectional electron transfer between NADP+ and F420H2 during the intestinal production of CH4 from CO2
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physiological function
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the enzyme catalyses the bidirectional electron transfer between NADP+ and F420H2 during the intestinal production of CH4 from CO2
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physiological function
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the enzyme catalyses the bidirectional electron transfer between NADP+ and F420H2 during the intestinal production of CH4 from CO2
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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
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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
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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
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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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additional information
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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
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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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