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Literature summary for 3.2.2.24 extracted from

  • Berthold, C.L.; Wang, H.; Nordlund, S.; Hoegbom, M.
    Mechanism of ADP-ribosylation removal revealed by the structure and ligand complexes of the dimanganese mono-ADP-ribosylhydrolase DraG (2009), Proc. Natl. Acad. Sci. USA, 106, 14247-14252.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.2.2.24

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant DraG in the holo and ADP-ribose bound forms and a reaction intermediate analogue, sitting drop vapor diffusion method, 0.0006 ml of of 10 mg/ml wild-type DraG is mixed with an equal volume of 15% PEG 3350, 0.3 M NH4Cl, and 0.1 M Tris, pH 7.0, several days, cryoprotection in 20% PEG 3350, 0.3 M NH4Cl, 0.1M Tris, pH 7.0, and 20% glycerol, X-ray diffraction structure determination and analysis at 2.2 A resolution, modelling, overview Rhodospirillum rubrum

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane DraG reversibly associates with the cell membrane Rhodospirillum rubrum 16020
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Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ two manganese ions per enzyme molecule bound at the active site, structure of the dinuclear binding site, overview. DraG shows a preference for manganese over magnesium, although not requiring a redox active metal for the reaction Rhodospirillum rubrum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ADP-ribosyl-[dinitrogen reductase] + H2O Rhodospirillum rubrum DraG removes ADP-ribose upon exposure of the bacteria to light or depletion of the nitrogen source added, regenerating the arginine guanidino group and activating the dinitrogenase reductase dimer ADP-ribose + [dinitrogen reductase]
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 ?
additional information Rhodospirillum rubrum DraG is capable of auto ADP-ribosylation when in excess of ADP-ribose, this reaction can function as an autoregulatory mechanism in vivo ?
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 ?

Organism

Organism UniProt Comment Textmining
Rhodospirillum rubrum P14300
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Reaction

Reaction Comment Organism Reaction ID
[dinitrogen reductase]-Nomega-alpha-(ADP-D-ribosyl)-L-arginine = ADP-D-ribose + [dinitrogen reductase]-L-arginine substrate binding structure and detailed catalytic mechanism for protein de-ADP-ribosylation involving ring opening of the substrate ribose, overview Rhodospirillum rubrum
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP-ribosyl-[dinitrogen reductase] + H2O
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 Rhodospirillum rubrum ADP-ribose + [dinitrogen reductase]
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 ?
ADP-ribosyl-[dinitrogen reductase] + H2O DraG removes ADP-ribose upon exposure of the bacteria to light or depletion of the nitrogen source added, regenerating the arginine guanidino group and activating the dinitrogenase reductase dimer Rhodospirillum rubrum ADP-ribose + [dinitrogen reductase]
-
 ?
additional information DraG is capable of auto ADP-ribosylation when in excess of ADP-ribose, this reaction can function as an autoregulatory mechanism in vivo Rhodospirillum rubrum ?
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 ?

Subunits

Subunits Comment Organism
monomer
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 Rhodospirillum rubrum

Synonyms

Synonyms Comment Organism
mono-ADP-ribosylhydrolase
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 Rhodospirillum rubrum

General Information

General Information Comment Organism
physiological function DraG is a key player in the regulation of nitrogenase activity. The enzyme, catalyzing removal of the ADP-ribose moiety, is involved in the reversible ADP-ribosylation, a ubiquitous regulatory posttranslational modification involved in numerous key processes such as DNA repair, transcription, cell differentiation, apoptosis, and the pathogenic mechanism of certain bacterial toxins Rhodospirillum rubrum