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Literature summary extracted from

  • Rubio, L.M.; Singer, S.W.; Ludden, P.W.
    Purification and characterization of NafY (apodinitrogenase gamma subunit) from Azotobacter vinelandii (2004), J. Biol. Chem., 279, 19739-19746.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.18.6.1 overexpression of Azotobacter vinelandii NafY protein in Escherichia coli strain BL21(DE3) Azotobacter vinelandii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.18.6.1 Iron enzyme contains an iron-molybdenum cofactor Azotobacter vinelandii
1.18.6.1 Molybdenum enzyme contains an iron-molybdenum cofactor Azotobacter vinelandii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.18.6.1 44000
-
FeMo cofactor-NafY protein complex, gel filtration Azotobacter vinelandii
1.18.6.1 46000
-
NafY protein, gel filtration, sedimentation equilibrium centrifugation Azotobacter vinelandii

Organism

EC Number Organism UniProt Comment Textmining
1.18.6.1 Azotobacter vinelandii
-
-
-
1.18.6.1 Azotobacter vinelandii DJ
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.18.6.1 recombinant Azotobacter vinelandii NafY protein from Escherichia coli strain BL21(DE3) Azotobacter vinelandii

Subunits

EC Number Subunits Comment Organism
1.18.6.1 dimer 2 * 26141-28000, unassociated NafY protein, sequence calculation and sedimentation equilibrium centrifugation Azotobacter vinelandii
1.18.6.1 More the NafY protein monomerizes upon binding to the FeMo cofactor Azotobacter vinelandii

Synonyms

EC Number Synonyms Comment Organism
1.18.6.1 More the nitrogenase complex is composed of 2 oxygen-labile metalloproteins: dinitrogenase and dinitrogenase reductase Azotobacter vinelandii

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.6.1 iron-molybdenum cofactor required for activity of the enzyme complex, insertion in the presynthesized apodinitrogenase involving the monomeric 26 kDa NafY protein, which binds the FeMo cofactor with very high affinity via its HIs121, the cofactor-NafY-complex exhibits an EPR signal similar to isolated FeMo cofactor and the M-center of the enzyme, NafY also binds the biosynthetic precursor of the MoFe cofactor, the NifB-cofacor, determination of binding sites Azotobacter vinelandii