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Literature summary extracted from

  • 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 (2020), Sci. Rep., 10, 13150 .
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.5.1.40 aphloiol
-
 Methanobrevibacter smithii
1.5.1.40 Baicalin
-
 Methanobrevibacter smithii
1.5.1.40 beta-D-glucose pentaacetate
-
 Methanobrevibacter smithii
1.5.1.40 frangulin A
-
 Methanobrevibacter smithii
1.5.1.40 mangiferin
-
 Methanobrevibacter smithii
1.5.1.40 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 Methanobrevibacter smithii
1.5.1.40 ononin
-
 Methanobrevibacter smithii
1.5.1.40 trans-5-O-caffeoyl-D-quinate
-
 Methanobrevibacter smithii
1.5.1.40 ZINC05409525
-
 Methanobrevibacter smithii
1.5.1.40 ZINC05409527
-
 Methanobrevibacter smithii
1.5.1.40 ZINC05409530
-
 Methanobrevibacter smithii
1.5.1.40 ZINC08951913
-
 Methanobrevibacter smithii
1.5.1.40 ZINC08951914
-
 Methanobrevibacter smithii
1.5.1.40 ZINC15449243
-
 Methanobrevibacter smithii
1.5.1.40 ZINC2120951
-
 Methanobrevibacter smithii
1.5.1.40 ZINC35442308
-
 Methanobrevibacter smithii
1.5.1.40 ZINC39205376
-
 Methanobrevibacter smithii
1.5.1.40 ZINC5449241
-
 Methanobrevibacter smithii
1.5.1.40 ZINC9271779
-
 Methanobrevibacter smithii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.1.40 reduced coenzyme F420 + NADP+ Methanobrevibacter smithii
-
 oxidized coenzyme F420 + NADPH + H+
-
 r
1.5.1.40 reduced coenzyme F420 + NADP+ Methanobrevibacter smithii DSM 861
-
 oxidized coenzyme F420 + NADPH + H+
-
 r
1.5.1.40 reduced coenzyme F420 + NADP+ Methanobrevibacter smithii OCM 144
-
 oxidized coenzyme F420 + NADPH + H+
-
 r
1.5.1.40 reduced coenzyme F420 + NADP+ Methanobrevibacter smithii PS
-
 oxidized coenzyme F420 + NADPH + H+
-
 r
1.5.1.40 reduced coenzyme F420 + NADP+ Methanobrevibacter smithii ATCC 35061
-
 oxidized coenzyme F420 + NADPH + H+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.40 Methanobrevibacter smithii A5UJ76
-
-
1.5.1.40 Methanobrevibacter smithii ATCC 35061 A5UJ76
-
-
1.5.1.40 Methanobrevibacter smithii DSM 861 A5UJ76
-
-
1.5.1.40 Methanobrevibacter smithii OCM 144 A5UJ76
-
-
1.5.1.40 Methanobrevibacter smithii PS A5UJ76
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.40 reduced coenzyme F420 + NADP+
-
 Methanobrevibacter smithii oxidized coenzyme F420 + NADPH + H+
-
 r
1.5.1.40 reduced coenzyme F420 + NADP+
-
 Methanobrevibacter smithii DSM 861 oxidized coenzyme F420 + NADPH + H+
-
 r
1.5.1.40 reduced coenzyme F420 + NADP+
-
 Methanobrevibacter smithii OCM 144 oxidized coenzyme F420 + NADPH + H+
-
 r
1.5.1.40 reduced coenzyme F420 + NADP+
-
 Methanobrevibacter smithii PS oxidized coenzyme F420 + NADPH + H+
-
 r
1.5.1.40 reduced coenzyme F420 + NADP+
-
 Methanobrevibacter smithii ATCC 35061 oxidized coenzyme F420 + NADPH + H+
-
 r

Synonyms

EC Number Synonyms Comment Organism
1.5.1.40 Fno
-
 Methanobrevibacter smithii
1.5.1.40 Msm_0049
-
 Methanobrevibacter smithii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.5.1.40 37
-
 assay at Methanobrevibacter smithii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.5.1.40 6
-
 assay at Methanobrevibacter smithii

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.40 NADP+
-
 Methanobrevibacter smithii
1.5.1.40 NADPH
-
 Methanobrevibacter smithii

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.5.1.40 0.000045
-
 Baicalin pH 6.0, 37°C Methanobrevibacter smithii
1.5.1.40 0.000047
-
 frangulin A pH 6.0, 37°C Methanobrevibacter smithii
1.5.1.40 0.000205
-
 ononin pH 6.0, 37°C Methanobrevibacter smithii
1.5.1.40 0.00021
-
 trans-5-O-caffeoyl-D-quinate pH 6.0, 37°C Methanobrevibacter smithii
1.5.1.40 0.00065
-
 mangiferin pH 6.0, 37°C Methanobrevibacter smithii
1.5.1.40 0.00097
-
 ZINC2120951 pH 6.0, 37°C Methanobrevibacter smithii
1.5.1.40 0.00107
-
 ZINC9271779 pH 6.0, 37°C Methanobrevibacter smithii
1.5.1.40 0.00122
-
 ZINC35442308 pH 6.0, 37°C Methanobrevibacter smithii
1.5.1.40 0.00396
-
 beta-D-glucose pentaacetate pH 6.0, 37°C Methanobrevibacter smithii

General Information

EC Number General Information Comment Organism
1.5.1.40 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 Methanobrevibacter smithii
1.5.1.40 physiological function the enzyme catalyses the bidirectional electron transfer between NADP+ and F420H2 during the intestinal production of CH4 from CO2 Methanobrevibacter smithii