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Literature summary 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)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.5.99.15 | expression in Escherichia coli | Methanosarcina mazei |
| 1.5.99.15 | expression in Escherichia coli | Methanocaldococcus jannaschii |
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 1.5.99.15 | stable when frozen in liquid nitrogen | Methanocaldococcus jannaschii |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.5.99.15 | Iron-sulfur cluster | iron-sulfur flavoprotein | Methanocaldococcus jannaschii |  |
| 1.5.99.15 | Iron-sulfur cluster | bioinformatic analysis reveals the presence of two iron-sulfur cluster sites | Methanosarcina mazei | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.5.99.15 | 29000 | - |
2 * 29000, SDS-PAGE | Methanosarcina mazei |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.5.99.15 | 7,8-dihydromethanopterin + reduced acceptor | Methanosarcina mazei | the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis | 5,6,7,8-tetrahydromethanopterin + oxidized acceptor | - |
? | |
| 1.5.99.15 | 7,8-dihydromethanopterin + reduced acceptor | Methanocaldococcus jannaschii | the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis | 5,6,7,8-tetrahydromethanopterin + oxidized acceptor | - |
? | |
| 1.5.99.15 | 7,8-dihydromethanopterin + reduced acceptor | Methanosarcina mazei DSM 3647 | the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis | 5,6,7,8-tetrahydromethanopterin + oxidized acceptor | - |
? | |
| 1.5.99.15 | 7,8-dihydromethanopterin + reduced acceptor | Methanocaldococcus jannaschii DSM 2661 | the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis | 5,6,7,8-tetrahydromethanopterin + oxidized acceptor | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.5.99.15 | Methanocaldococcus jannaschii | Q57661 | - |
- |
| 1.5.99.15 | Methanocaldococcus jannaschii DSM 2661 | Q57661 | - |
- |
| 1.5.99.15 | Methanosarcina mazei | Q8PVV3 | - |
- |
| 1.5.99.15 | Methanosarcina mazei DSM 3647 | Q8PVV3 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.5.99.15 | - |
Methanosarcina mazei |
| 1.5.99.15 | - |
Methanocaldococcus jannaschii |
Storage Stability
| EC Number | Storage Stability | Organism |
|---|---|---|
| 1.5.99.15 | labile when exposed to cold storage at 4°C and 20°C or liquid nitrogen temperatures | Methanosarcina mazei |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.5.99.15 | 7,8-dihydromethanopterin + reduced acceptor | the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis | Methanosarcina mazei | 5,6,7,8-tetrahydromethanopterin + oxidized acceptor | - |
? | |
| 1.5.99.15 | 7,8-dihydromethanopterin + reduced acceptor | the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis | Methanocaldococcus jannaschii | 5,6,7,8-tetrahydromethanopterin + oxidized acceptor | - |
? | |
| 1.5.99.15 | 7,8-dihydromethanopterin + reduced acceptor | the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis | Methanosarcina mazei DSM 3647 | 5,6,7,8-tetrahydromethanopterin + oxidized acceptor | - |
? | |
| 1.5.99.15 | 7,8-dihydromethanopterin + reduced acceptor | the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis | Methanocaldococcus jannaschii DSM 2661 | 5,6,7,8-tetrahydromethanopterin + oxidized acceptor | - |
? | |
| 1.5.99.15 | 7,8-dihydromethanopterin + reduced dithiothreitol | - |
Methanocaldococcus jannaschii | 5,6,7,8-tetrahydromethanopterin + oxidized dithiothreitol | - |
? | |
| 1.5.99.15 | 7,8-dihydromethanopterin + reduced dithiothreitol | NAD(P)H is incapable of directly reducing the flavin cofactor, but dithionite eliminates the FMN peaks, indicating successful electron transfer to the enzyme. An electron transfer system of NADPH, spinach NADPH-ferredoxin oxidoreductase, and ferredoxin can also reduce the FMN peaks. A newly developed assay indicates that dithiothreitol-reduced enzyme can transfer electrons to dihydromethanopterin. Ferredoxin may serve as an electron donor | Methanosarcina mazei | 5,6,7,8-tetrahydromethanopterin + oxidized dithiothreitol | - |
? | |
| 1.5.99.15 | 7,8-dihydromethanopterin + reduced dithiothreitol | NAD(P)H is incapable of directly reducing the flavin cofactor, but dithionite eliminates the FMN peaks, indicating successful electron transfer to the enzyme. An electron transfer system of NADPH, spinach NADPH-ferredoxin oxidoreductase, and ferredoxin can also reduce the FMN peaks. A newly developed assay indicates that dithiothreitol-reduced enzyme can transfer electrons to dihydromethanopterin. Ferredoxin may serve as an electron donor | Methanosarcina mazei DSM 3647 | 5,6,7,8-tetrahydromethanopterin + oxidized dithiothreitol | - |
? | |
| 1.5.99.15 | 7,8-dihydromethanopterin + reduced dithiothreitol | - |
Methanocaldococcus jannaschii DSM 2661 | 5,6,7,8-tetrahydromethanopterin + oxidized dithiothreitol | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.5.99.15 | homodimer | 2 * 29000, SDS-PAGE | Methanosarcina mazei |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.5.99.15 | DmrX | - |
Methanosarcina mazei |
| 1.5.99.15 | DmrX | - |
Methanocaldococcus jannaschii |
| 1.5.99.15 | MJ0208 | locus name | Methanocaldococcus jannaschii |
| 1.5.99.15 | MM1854 | locus name | Methanosarcina mazei |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.5.99.15 | flavin | iron-sulfur flavoprotein | Methanocaldococcus jannaschii | |
| 1.5.99.15 | FMN | bioinformatic analysis reveals the presence of one FMN-binding site. The purified protein shows an absorbance peaks at 380 and 460 nm, characteristic of oxidized FMN | Methanosarcina mazei | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.5.99.15 | physiological function | the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis | Methanosarcina mazei |
| 1.5.99.15 | physiological function | the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis | Methanocaldococcus jannaschii |
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Release 2023.1 (January 2023)
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