Any feedback?
Literature summary extracted from
- Purification and properties of 5,10-methylenetetrahydrofolate reductase from Clostridium formicoaceticum (1986), Methods Enzymol., 122, 392-399.
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 1.5.1.20 | 0.005 mM FAD stabilizes enzyme during purification procedure | Clostridium formicaceticum |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.5.1.20 | 0.12 | - |
5-methyltetrahydrofolate | - |
Clostridium formicaceticum |  |
| 1.5.1.20 | 11.1 | - |
benzyl viologen | - |
Clostridium formicaceticum | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.5.1.20 | Iron | 15.2 molecules iron per enzyme molecule, enzyme contains iron-sulfur clusters | Clostridium formicaceticum | |
| 1.5.1.20 | iron-sulfur centre | enzyme contains 15.2 molecules iron and 19.5 molecules acid-labile sulfur as iron-sulfur clusters | Clostridium formicaceticum | |
| 1.5.1.20 | Zinc | 2.3 molecules zinc per enzyme molecule | Clostridium formicaceticum | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.5.1.20 | 26000 | - |
alpha4,beta4, 4 * 26000 + 4 * 35000, SDS-PAGE | Clostridium formicaceticum |
| 1.5.1.20 | 35000 | - |
alpha4,beta4, 4 * 26000 + 4 * 35000, SDS-PAGE | Clostridium formicaceticum |
| 1.5.1.20 | 237000 | - |
gel filtration | Clostridium formicaceticum |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.5.1.20 | 5,10-methylenetetrahydrofolate + reduced ferredoxin | Clostridium formicaceticum | physiological important reaction: enzyme catalyzes reduction of 5,10-methylenetetrahydrofolate with reduced ferredoxin | 5-methyltetrahydrofolate + oxidized ferredoxin | - |
? | |
| 1.5.1.20 | 5,10-methylenetetrahydrofolate + reduced ferredoxin | Clostridium formicaceticum | enzyme is part of synthesis pathway of acetate from CO2 via a unique tetrahydrofolate-corrinoid pathway | 5-methyltetrahydrofolate + oxidized ferredoxin | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.5.1.20 | Clostridium formicaceticum | - |
strain ATCC 23439 | - |
Oxidation Stability
| EC Number | Oxidation Stability | Organism |
|---|---|---|
| 1.5.1.20 | oxygen labile, half-life: less than 1 h in aerobic buffer, sodium dithionite prevents inactivation by oxygen | Clostridium formicaceticum |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.5.1.20 | - |
Clostridium formicaceticum |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.5.1.20 | 139 | - |
- |
Clostridium formicaceticum |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.5.1.20 | 5,10-methylenetetrahydrofolate + reduced acceptor | forward reaction: reduced acceptor is FADH2 | Clostridium formicaceticum | 5-methyltetrahydrofolate + oxidized acceptor | - |
r | |
| 1.5.1.20 | 5,10-methylenetetrahydrofolate + reduced acceptor | reverse reaction: menadione as electron acceptor | Clostridium formicaceticum | 5-methyltetrahydrofolate + oxidized acceptor | - |
r | |
| 1.5.1.20 | 5,10-methylenetetrahydrofolate + reduced acceptor | reverse reaction: FAD, rubredoxin, benzyl viologen and methylene blue as electron acceptor | Clostridium formicaceticum | 5-methyltetrahydrofolate + oxidized acceptor | - |
r | |
| 1.5.1.20 | 5,10-methylenetetrahydrofolate + reduced acceptor | forward reaction: reduced ferredoxin as reduced acceptor | Clostridium formicaceticum | 5-methyltetrahydrofolate + oxidized acceptor | - |
r | |
| 1.5.1.20 | 5,10-methylenetetrahydrofolate + reduced ferredoxin | physiological important reaction: enzyme catalyzes reduction of 5,10-methylenetetrahydrofolate with reduced ferredoxin | Clostridium formicaceticum | 5-methyltetrahydrofolate + oxidized ferredoxin | - |
? | |
| 1.5.1.20 | 5,10-methylenetetrahydrofolate + reduced ferredoxin | enzyme is part of synthesis pathway of acetate from CO2 via a unique tetrahydrofolate-corrinoid pathway | Clostridium formicaceticum | 5-methyltetrahydrofolate + oxidized ferredoxin | - |
? | |
| 1.5.1.20 | 5-methyltetrahydrofolate + NAD+ | - |
Clostridium formicaceticum | 5,10-methylenetetrahydrofolate + NADH + H+ | - |
r | |
| 1.5.1.20 | additional information | no direct activity with pyridine nucleotides | Clostridium formicaceticum | ? | - |
? | |
| 1.5.1.20 | additional information | not as electron donor: reduced rubredoxin | Clostridium formicaceticum | ? | - |
? | |
| 1.5.1.20 | nitrate + reduced benzyl viologen | - |
Clostridium formicaceticum | nitrite + benzyl viologen | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.5.1.20 | octamer | alpha4,beta4, 4 * 26000 + 4 * 35000, SDS-PAGE | Clostridium formicaceticum |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.5.1.20 | FAD | 1.7 molecules enzyme-bound FAD per enzyme molecule | Clostridium formicaceticum | |
| 1.5.1.20 | FAD | flavoprotein, oxidized acceptor in reverse reaction | Clostridium formicaceticum | |
| 1.5.1.20 | FADH2 | flavoprotein, reduced acceptor in forward reaction | Clostridium formicaceticum | |
| 1.5.1.20 | additional information | no direct activity with pyridine nucleotides: NADH, NADPH | Clostridium formicaceticum |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
