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Literature summary for 1.5.99.15 extracted from
- Discovery and characterization of the first archaeal dihydromethanopterin reductase, an iron-sulfur flavoprotein from Methanosarcina mazei (2014), J. Bacteriol., 196, 203-209 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene dmrX, recombinant expression of His6-tagged enzyme in Escherichia coli strain BE100 [BL21(DE3) RIL] | Methanosarcina mazei |
| gene dmrX, recombinant expression of the codon-optimized gene encoding His6-tagged enzyme in Escherichia col strain BE100 [BL21(DE3) RIL] | Methanocaldococcus jannaschii |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | the enzyme contains two [4Fe-4S] cluster sites | Methanosarcina mazei |  |
| Fe2+ | the enzyme contains two [4Fe-4S] cluster sites | Methanocaldococcus jannaschii | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 7,8-dihydromethanopterin + reduced ferredoxin | Methanosarcina mazei | - |
5,6,7,8-tetrahydromethanopterin + ferredoxin | - |
? | |
| 7,8-dihydromethanopterin + reduced ferredoxin | Methanocaldococcus jannaschii | - |
5,6,7,8-tetrahydromethanopterin + ferredoxin | - |
? | |
| 7,8-dihydromethanopterin + reduced ferredoxin | Methanosarcina mazei DSM 3647 | - |
5,6,7,8-tetrahydromethanopterin + ferredoxin | - |
? | |
| 7,8-dihydromethanopterin + reduced ferredoxin | Methanocaldococcus jannaschii DSM 2661 | - |
5,6,7,8-tetrahydromethanopterin + ferredoxin | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methanocaldococcus jannaschii | Q57661 | - |
- |
| Methanocaldococcus jannaschii DSM 2661 | Q57661 | - |
- |
| Methanosarcina mazei | Q8PVV3 | - |
- |
| Methanosarcina mazei DSM 3647 | Q8PVV3 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His6-tagged enzyme from Escherichia col strain BE100 [BL21(DE3) RIL] in an anaerobic chamber by heat treatement at 65°C for 5 min, the supernatant is a second time heat treated at 85°C for 15 min, | Methanocaldococcus jannaschii |
| recombinant His6-tagged enzyme from Escherichia coli strain BE100 [BL21(DE3) RIL] in an anaerobic chamber by nickel affinity chromatography, ultrafiltration, and gel filtration | Methanosarcina mazei |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 7,8-dihydromethanopterin + reduced ferredoxin | - |
Methanosarcina mazei | 5,6,7,8-tetrahydromethanopterin + ferredoxin | - |
? | |
| 7,8-dihydromethanopterin + reduced ferredoxin | - |
Methanocaldococcus jannaschii | 5,6,7,8-tetrahydromethanopterin + ferredoxin | - |
? | |
| 7,8-dihydromethanopterin + reduced ferredoxin | - |
Methanosarcina mazei DSM 3647 | 5,6,7,8-tetrahydromethanopterin + ferredoxin | - |
? | |
| 7,8-dihydromethanopterin + reduced ferredoxin | - |
Methanocaldococcus jannaschii DSM 2661 | 5,6,7,8-tetrahydromethanopterin + ferredoxin | - |
? | |
| additional information | NAD(P)H is incapable of directly reducing the flavin cofactor, but dithionite eliminates the FMN peaks, indicating successful electron transfer to MJ0208. An electron transfer system of NADPH, spinach NADPH-ferredoxin oxidoreductase, and ferredoxin can also reduce the FMN peaks. Dithiothreitol-reduced MJ0208 can transfer electrons to dihydromethanopterin | Methanocaldococcus jannaschii | ? | - |
? | |
| additional information | NAD(P)H is incapable of directly reducing the flavin cofactor, but dithionite eliminates the FMN peaks, indicating successful electron transfer to MM1854. An electron transfer system of NADPH, spinach NADPH-ferredoxin oxidoreductase, and ferredoxin can also reduce the FMN peaks. Dithiothreitol-reduced MM1854 can transfer electrons to dihydromethanopterin | Methanosarcina mazei | ? | - |
? | |
| additional information | NAD(P)H is incapable of directly reducing the flavin cofactor, but dithionite eliminates the FMN peaks, indicating successful electron transfer to MM1854. An electron transfer system of NADPH, spinach NADPH-ferredoxin oxidoreductase, and ferredoxin can also reduce the FMN peaks. Dithiothreitol-reduced MM1854 can transfer electrons to dihydromethanopterin | Methanosarcina mazei DSM 3647 | ? | - |
? | |
| additional information | NAD(P)H is incapable of directly reducing the flavin cofactor, but dithionite eliminates the FMN peaks, indicating successful electron transfer to MJ0208. An electron transfer system of NADPH, spinach NADPH-ferredoxin oxidoreductase, and ferredoxin can also reduce the FMN peaks. Dithiothreitol-reduced MJ0208 can transfer electrons to dihydromethanopterin | Methanocaldococcus jannaschii DSM 2661 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | 2 * 29000, recombinant His6-tagged enzyme, SDS-PAGE | Methanosarcina mazei |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AfpA | - |
Methanocaldococcus jannaschii |
| archaeal-flavoprotein-like flavoprotein | - |
Methanocaldococcus jannaschii |
| DmrX | - |
Methanosarcina mazei |
| DmrX | - |
Methanocaldococcus jannaschii |
| methylene H4MPT dehydrogenase B | - |
Methanosarcina mazei |
| MJ0208 | - |
Methanocaldococcus jannaschii |
| MM1854 | - |
Methanosarcina mazei |
| MtdB | - |
Methanosarcina mazei |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 22 | - |
assay at room temperature | Methanosarcina mazei |
| 22 | - |
assay at room temperature | Methanocaldococcus jannaschii |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 100 | - |
purified recombinant His-tagged enzyme, pH 7.0, 15 min, inactivation | Methanosarcina mazei |
| 100 | - |
purified recombinant His-tagged enzyme, pH 7.0, 15 min, inactivation | Methanocaldococcus jannaschii |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | 7.5 | - |
Methanosarcina mazei |
| 7 | 7.5 | - |
Methanocaldococcus jannaschii |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| Ferredoxin | ferredoxin may serve as an electron donor | Methanosarcina mazei | |
| Ferredoxin | ferredoxin may serve as an electron donor | Methanocaldococcus jannaschii | |
| FMN | the enzyme contains one flavin mononucleotide (FMN)-binding site | Methanosarcina mazei | |
| FMN | the enzyme contains one flavin mononucleotide (FMN)-binding site | Methanocaldococcus jannaschii | |
| additional information | NAD(P)H is incapable of directly reducing the flavin cofactor, but dithionite eliminates the FMN peaks, indicating successful electron transfer to MJ0208. An electron transfer system of NADPH, spinach NADPH-ferredoxin oxidoreductase, and ferredoxin can also reduce the FMN peaks. Dithiothreitol-reduced MJ0208 can transfer electrons to dihydromethanopterin | Methanocaldococcus jannaschii | |
| additional information | NAD(P)H is incapable of directly reducing the flavin cofactor, but dithionite eliminates the FMN peaks, indicating successful electron transfer to MM1854. An electron transfer system of NADPH, spinach NADPH-ferredoxin oxidoreductase, and ferredoxin can also reduce the FMN peaks. Dithiothreitol-reduced MM1854 can transfer electrons to dihydromethanopterin | Methanosarcina mazei | |
| [4Fe-4S]-center | the enzyme contains two iron-sulfur cluster sites | Methanosarcina mazei | |
| [4Fe-4S]-center | the enzyme contains two iron-sulfur cluster sites | Methanocaldococcus jannaschii | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | the microbial production of methane by methanogenic archaea is dependent on the synthesis of the pterin-containing cofactor tetrahydromethanopterin (H4MPT). The enzyme catalyzing the last step of H4MPT biosynthesis is dihydromethanopterin reductase | Methanosarcina mazei |
| metabolism | the microbial production of methane by methanogenic archaea is dependent on the synthesis of the pterin-containing cofactor tetrahydromethanopterin (H4MPT). The enzyme catalyzing the last step of H4MPT biosynthesis is dihydromethanopterin reductase | Methanocaldococcus jannaschii |
| physiological function | MJ0208 functions as an archaeal dihydromethanopterin reductase (DmrX) and ferredoxin may serve as an electron donor | Methanocaldococcus jannaschii |
| physiological function | MM1854 functions as an archaeal dihydromethanopterin reductase (DmrX) and ferredoxin may serve as an electron donor | Methanosarcina mazei |
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