Any feedback?
Literature summary for 2.8.4.1 extracted from
- The nickel enzyme methyl-coenzyme M reductase from methanogenic archaea: in vitro interconversions among the EPR detectable MCR-red1 and MCR-red2 states (2002), J. Biol. Inorg. Chem., 7, 101-112.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ni | enzyme contains the tightly-bound nickel porphinol F-430 as prosthetic group | Methanothermobacter marburgensis |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methanothermobacter marburgensis | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Methanothermobacter marburgensis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| F-430 | tightly bound nickel porphinol. The enzyme is active only when its prosthetic group in in the NI(I)-reduced state | Methanothermobacter marburgensis | |
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
