Literature summary for 3.2.2.24 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.

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Organism

Organism	UniProt	Comment	Textmining
Rhodospirillum rubrum	-	-	-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	-	?
additional information	activity depends on oxidation state of Fe protein, with reduced Fe protein about 2% of activity compared to oxidized substrate	Rhodospirillum rubrum	?	-	?
Nalpha-dansyl-Nomega-(1,N6-etheno-ADP-ribosyl)-arginine methyl ester	-	Rhodospirillum rubrum	ADP-ribose + Nalpha-dansyl-Nomega-(1,N6-ethyl)-arginine methyl ester	-	?

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Release 2023.1 (January 2023)