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Literature summary extracted from

  • Moure, V.R.; Danyal, K.; Yang, Z.Y.; Wendroth, S.; Mueller-Santos, M.; Pedrosa, F.O.; Scarduelli, M.; Gerhardt, E.C.; Huergo, L.F.; Souza, E.M.; Seefeldt, L.C.
    The nitrogenase regulatory enzyme dinitrogenase reductase ADP-ribosyltransferase (DraT) is activated by direct interaction with the signal transduction protein GlnB (2013), J. Bacteriol., 195, 279-286.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.4.2.37 protein GlnB GlnB, a nitrogen-signaling PII protein, is necessary for DraT activity in the presence of Mg-ADP Azospirillum brasilense
2.4.2.37 protein GlnZ GlnZ, a nitrogen-signaling PII protein, activates DraT activity Azospirillum brasilense

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.2.37 2-oxoglutarate
-
 Azospirillum brasilense

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.2.37 0.166
-
 NAD+ pH 7.5, 30°C, Fe protein as the acceptor of ADP-ribose, in the presence of MgADP- Azospirillum brasilense

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.2.37 Mg2+ MgADP- required. DraT-GlnB is ineffective in the presence of MgATP2- Azospirillum brasilense

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.2.24 32000
-
 1 * 32000, SDS-PAGE Rhodospirillum rubrum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.2.24 ADP-D-ribosyl-[dinitrogen reductase] Rhodospirillum rubrum
-
 ADP-D-ribose + [dinitrogen reductase]
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.37 Azospirillum brasilense Q9JP48
-
-
3.2.2.24 Rhodospirillum rubrum
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.2.37 NAD+ + dinitrogen reductase Fe protein as the acceptor of ADP-ribose Azospirillum brasilense nicotinamide + ADP-D-ribosyl-[dinitrogen reductase]
-
 ?
3.2.2.24 ADP-D-ribosyl-[dinitrogen reductase]
-
 Rhodospirillum rubrum ADP-D-ribose + [dinitrogen reductase]
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.2.24 monomer 1 * 32000, SDS-PAGE Rhodospirillum rubrum

Synonyms

EC Number Synonyms Comment Organism
2.4.2.37 dinitrogenase reductase ADP-ribosyltransferase
-
 Azospirillum brasilense
2.4.2.37 DRAT
-
 Azospirillum brasilense
3.2.2.24 dinitrogenase reductase-activating glycohydrolase
-
 Rhodospirillum rubrum
3.2.2.24 DRAG
-
 Rhodospirillum rubrum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.2.37 30
-
 assay at Azospirillum brasilense

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.4.2.37 0.501
-
 NAD+ pH 7.5, 30°C, Fe protein as the acceptor of ADP-ribose, in the presence of MgADP- Azospirillum brasilense

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.2.37 7.5
-
 assay at Azospirillum brasilense

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.4.2.37 additional information
-
 additional information the DraT-GlnB complex is at least 18fold more efficient than DraT purified from Rhodospirillum rubrum Azospirillum brasilense
2.4.2.37 3.018
-
 NAD+ pH 7.5, 30°C, Fe protein as the acceptor of ADP-ribose, in the presence of MgADP- Azospirillum brasilense