Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Methanosarcina mazei |
expression in Escherichia coli | Methanocaldococcus jannaschii |
General Stability | Organism |
---|---|
stable when frozen in liquid nitrogen | Methanocaldococcus jannaschii |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Iron-sulfur cluster | iron-sulfur flavoprotein | Methanocaldococcus jannaschii | |
Iron-sulfur cluster | bioinformatic analysis reveals the presence of two iron-sulfur cluster sites | Methanosarcina mazei |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
29000 | - |
2 * 29000, SDS-PAGE | Methanosarcina mazei |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
7,8-dihydromethanopterin + reduced acceptor | Methanosarcina mazei | the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis | 5,6,7,8-tetrahydromethanopterin + oxidized acceptor | - |
? | |
7,8-dihydromethanopterin + reduced acceptor | Methanocaldococcus jannaschii | the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis | 5,6,7,8-tetrahydromethanopterin + oxidized acceptor | - |
? | |
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 | - |
? | |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Methanocaldococcus jannaschii | Q57661 | - |
- |
Methanocaldococcus jannaschii DSM 2661 | Q57661 | - |
- |
Methanosarcina mazei | Q8PVV3 | - |
- |
Methanosarcina mazei DSM 3647 | Q8PVV3 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Methanosarcina mazei |
- |
Methanocaldococcus jannaschii |
Storage Stability | Organism |
---|---|
labile when exposed to cold storage at 4°C and 20°C or liquid nitrogen temperatures | Methanosarcina mazei |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
7,8-dihydromethanopterin + reduced acceptor | the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis | Methanosarcina mazei | 5,6,7,8-tetrahydromethanopterin + oxidized acceptor | - |
? | |
7,8-dihydromethanopterin + reduced acceptor | the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis | Methanocaldococcus jannaschii | 5,6,7,8-tetrahydromethanopterin + oxidized acceptor | - |
? | |
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 | - |
? | |
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 | - |
? | |
7,8-dihydromethanopterin + reduced dithiothreitol | - |
Methanocaldococcus jannaschii | 5,6,7,8-tetrahydromethanopterin + oxidized dithiothreitol | - |
? | |
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 | - |
? | |
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 | - |
? | |
7,8-dihydromethanopterin + reduced dithiothreitol | - |
Methanocaldococcus jannaschii DSM 2661 | 5,6,7,8-tetrahydromethanopterin + oxidized dithiothreitol | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | 2 * 29000, SDS-PAGE | Methanosarcina mazei |
Synonyms | Comment | Organism |
---|---|---|
DmrX | - |
Methanosarcina mazei |
DmrX | - |
Methanocaldococcus jannaschii |
MJ0208 | locus name | Methanocaldococcus jannaschii |
MM1854 | locus name | Methanosarcina mazei |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
flavin | iron-sulfur flavoprotein | Methanocaldococcus jannaschii | |
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 | Comment | Organism |
---|---|---|
physiological function | the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis | Methanosarcina mazei |
physiological function | the enzyme catalyzes the last step of tetrahydromethanopterin biosynthesis | Methanocaldococcus jannaschii |