| EC |
2.4.2.37 |
| Accepted name: |
NAD+—dinitrogen-reductase ADP-D-ribosyltransferase |
| Reaction: |
NAD+ + [dinitrogen reductase]-L-arginine = nicotinamide + [dinitrogen reductase]-Nω-α-(ADP-D-ribosyl)-L-arginine |
| Other name(s): |
NAD-azoferredoxin (ADPribose)transferase; NAD-dinitrogen-reductase ADP-D-ribosyltransferase; draT (gene name) |
| Systematic name: |
NAD+:[dinitrogen reductase] (ADP-D-ribosyl)transferase |
| Comments: |
The combined action of this enzyme and EC 3.2.2.24, ADP-ribosyl-[dinitrogen reductase] hydrolase, controls the activity level of nitrogenase (EC 1.18.6.1). In the presence of ammonium, the product of nitrogenase, this enzyme covalently links an ADP-ribose moiety to a specific arginine residue of the dinitrogenase reductase component of nitrogenase, blocking its activity. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 117590-45-1 |
| References: |
| 1. |
Lowery, R.G. and Ludden, P.W. Purification and properties of dinitrogenase reductase ADP-ribosyltransferase from the photosynthetic bacterium Rhodospirillum rubrum. J. Biol. Chem. 263 (1988) 16714–16719. [PMID: 3141411] |
| 2. |
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] |
| 3. |
Moure, V.R., Costa, F.F., Cruz, L.M., Pedrosa, F.O., Souza, E.M., Li, X.D., Winkler, F. and Huergo, L.F. Regulation of nitrogenase by reversible mono-ADP-ribosylation. Curr. Top. Microbiol. Immunol. 384 (2015) 89–106. [DOI] [PMID: 24934999] |
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| [EC 2.4.2.37 created 1992, modified 2015] |
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