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Literature summary for 1.5.1.40 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
Search for more literature for 1.5.1.40

Inhibitors

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
Fno
-
 Methanobrevibacter smithii
Msm_0049
-
 Methanobrevibacter smithii

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
NADP+
-
 Methanobrevibacter smithii
NADPH
-
 Methanobrevibacter smithii

Ki Value [mM]

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

General Information

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