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 | 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 | 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 | Comment | Organism | Textmining |
---|
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 | Comment | Organism |
---|---|---|
Fno | - |
Methanobrevibacter smithii |
Msm_0049 | - |
Methanobrevibacter smithii |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Methanobrevibacter smithii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
assay at | Methanobrevibacter smithii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADP+ | - |
Methanobrevibacter smithii | |
NADPH | - |
Methanobrevibacter smithii |
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 | 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 |