EC - ADP-ribosyl-[dinitrogen reductase] hydrolase

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IntEnz Enzyme Nomenclature


Accepted name:
ADP-ribosyl-[dinitrogen reductase] hydrolase
Other names:
ADP-ribosyl glycohydrolase
azoferredoxin glycosidase
azoferredoxin-activating enzymes
dinitrogenase reductase-activating glycohydrolase
dinitrogenase reductase activating glycohydrolase
draG (gene name)
Systematic name:
ADP-D-ribosyl-[dinitrogen reductase] ADP-ribosylhydrolase



The enzyme restores the activity of EC, nitrogenase, by catalysing the removal of ADP-ribose from an arginine residue of the dinitrogenase reductase component of nitrogenase. This activity occurs only when the nitrogenase product, ammonium, is not available. The combined activity of this enzyme and EC, NAD+-dinitrogen-reductase ADP-D-ribosyltransferase, controls the level of activity of nitrogenase.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0047407


  1. Fitzmaurice, W.P., Saari, L.L., Lowery, R.G., Ludden, P.W. and Roberts, G.P.
    Genes coding for the reversible ADP-ribosylation system of dinitrogenase reductase from Rhodospirillum rubrum.
    Mol. Gen. Genet. 218: 340-347 (1989). [PMID: 2506427]
  2. Li, X. D., Huergo, L. F., Gasperina, A., Pedrosa, F. O., Merrick, M., Winkler, F. K.
    Crystal structure of dinitrogenase reductase-activating glycohydrolase (DraG) reveals conservation in the ADP-ribosylhydrolase fold and specific features in the ADP-ribose-binding pocket.
    J. Mol. Biol. 390: 737-746 (2009). [PMID: 19477184]
  3. Berthold, C. L., Wang, H., Nordlund, S., Hogbom, M.
    Mechanism of ADP-ribosylation removal revealed by the structure and ligand complexes of the dimanganese mono-ADP-ribosylhydrolase DraG.
    Proc. Natl. Acad. Sci. U.S.A. 106: 14247-14252 (2009). [PMID: 19706507]

[EC created 1992]