The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

Accepted name: ADP-ribosyl-[dinitrogen reductase] hydrolase
Reaction: [dinitrogen reductase]-Nω-α-(ADP-D-ribosyl)-L-arginine = ADP-D-ribose + [dinitrogen reductase]-L-arginine
Other name(s): azoferredoxin glycosidase; azoferredoxin-activating enzymes; dinitrogenase reductase-activating glycohydrolase; ADP-ribosyl glycohydrolase; draG (gene name)
Systematic name: ADP-D-ribosyl-[dinitrogen reductase] ADP-ribosylhydrolase
Comments: 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: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 125626-63-3
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 (1989) 340–347. [PMID: 2506427]
2.  Li, X.D., Huergo, L.F., Gasperina, A., Pedrosa, F.O., Merrick, M. and 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 (2009) 737–746. [DOI] [PMID: 19477184]
3.  Berthold, C.L., Wang, H., Nordlund, S. and 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. USA 106 (2009) 14247–14252. [DOI] [PMID: 19706507]
[EC created 1992]

Data © 2001–2023 IUBMB
Web site © 2005–2023 Andrew McDonald