Literature summary extracted from
Kaiser, J.T.; Hu, Y.; Wiig, J.A.; Rees, D.C.; Ribbe, M.W.
Structure of precursor-bound NifEN: a nitrogenase FeMo cofactor maturase/insertase (2011), Science, 331, 91-94.
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
1.18.6.1 |
Iron |
in the FeMo cofactor |
Azotobacter vinelandii |
|
1.18.6.1 |
Molybdenum |
in the FeMo cofactor |
Azotobacter vinelandii |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.18.6.1 |
Azotobacter vinelandii |
- |
- |
- |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.18.6.1 |
FeMo cofactor |
NifEN plays an essential role in the biosynthesis of the nitrogenase iron-molybdenum, FeMo, cofactor. It is an alpha2beta2 tetramer that is homologous to the catalytic MoFe protein, NifDK, component of nitrogenase. NifEN serves as a scaffold for the conversion of an iron-only precursor to a matured form of the M cluster before delivering the latter to its target location within NifDK, NifEN crystal structure analysis, overview |
Azotobacter vinelandii |
|
General Information
EC Number |
General Information |
Comment |
Organism |
---|
1.18.6.1 |
additional information |
NifEN plays an essential role in the biosynthesis of the nitrogenase iron-molybdenum, FeMo, cofactor. It is an alpha2beta2 tetramer that is homologous to the catalytic MoFe protein, NifDK, component of nitrogenase. NifEN serves as a scaffold for the conversion of an iron-only precursor to a matured form of the M cluster before delivering the latter to its target location within NifDK, NifEN crystal structure analysis, overview |
Azotobacter vinelandii |