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Literature summary extracted from

  • Halbleib, C.M.; Zhang, Y.; Ludden, P.W.
    Regulation of dinitrogenase reductase ADP-ribosyltransferase and dinitrogenase reductase-activating glycohydrolase by a redox-dependent conformational change of nitrogenase Fe protein (2000), J. Biol. Chem., 275, 3493-3500.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.2.37 additional information
-
 additional information activity of enzyme depends on the redox status of the Fe4S41+/2+ cluster of nitrogenase Fe protein Rhodospirillum rubrum

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.37 Rhodospirillum rubrum
-
-
-
3.2.2.24 Rhodospirillum rubrum
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.2.24 additional information
-
 model of enzyme regulation Rhodospirillum rubrum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.2.24 ADP-D-ribosyl-(dinitrogen reductase) component of nitrogenase complex enzyme is sensitive to the redox-state of the (Fe4S4) cluster of substrate protein, having less than 2% of activity with oxidized Fe protein compared to reduced Fe protein Rhodospirillum rubrum ADP-ribose + (dinitrogen reductase) component of nitrogenase complex
-
 ?
3.2.2.24 additional information activity depends on oxidation state of Fe protein, with reduced Fe protein about 2% of activity compared to oxidized substrate Rhodospirillum rubrum ?
-
 ?
3.2.2.24 Nalpha-dansyl-Nomega-(1,N6-etheno-ADP-ribosyl)-arginine methyl ester
-
 Rhodospirillum rubrum ADP-ribose + Nalpha-dansyl-Nomega-(1,N6-ethyl)-arginine methyl ester
-
 ?