EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   1.5.99.15 | 5,6,7,8-tetrahydromethanopterin + oxidized acceptor |
- |
Paraburkholderia xenovorans |
7,8-dihydromethanopterin + reduced acceptor |
- |
? |
| 1.5.99.15 | 7,8-dihydromethanopterin + FMNH2 |
- |
Paraburkholderia xenovorans |
5,6,7,8-tetrahydromethanopterin + FMN |
- |
? |
| 1.5.99.15 | 7,8-dihydromethanopterin + FMNH2 |
DmrB uses a ping-pong mechanism to transfer reducing equivalents from FMN to the pterin substrate, identification of the 7,8-dihydromethanopterin binding site by computational docking |
Paraburkholderia xenovorans |
5,6,7,8-tetrahydromethanopterin + FMN |
- |
? |
| 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 |
- |
? |
