Information on EC 2.4.2.37 - NAD+-dinitrogen-reductase ADP-D-ribosyltransferase

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The expected taxonomic range for this enzyme is: Alphaproteobacteria

EC NUMBER
COMMENTARY hide
2.4.2.37
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RECOMMENDED NAME
GeneOntology No.
NAD+-dinitrogen-reductase ADP-D-ribosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NAD+ + [dinitrogen reductase]-L-arginine = nicotinamide + [dinitrogen reductase]-Nomega-alpha-(ADP-D-ribosyl)-L-arginine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentosyl group transfer
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-
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SYSTEMATIC NAME
IUBMB Comments
NAD+:[dinitrogen reductase] (ADP-D-ribosyl)transferase
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.
CAS REGISTRY NUMBER
COMMENTARY hide
117590-45-1
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
mutation of draT2 results in inactivation of the nitrogenase posttranslational modification system and in increased H2 production by ammonium-grown NifA cells
physiological function
DraT2 and GlnK2, an NtrC-regulated PII protein, are involved in posttranslational regulation of nitrogenase activity in Rhodopseudomonas palustris
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
etheno-NAD+ + [dinitrogen reductase]
?
show the reaction diagram
-
-
-
-
?
NAD+ + dinitrogen reductase
nicotinamide + ADP-D-ribosyl-[dinitrogen reductase]
show the reaction diagram
Fe protein as the acceptor of ADP-ribose
-
-
?
NAD+ + [dinitrogen reductase]
?
show the reaction diagram
NAD+ + [dinitrogen reductase]
nicotinamide + ADP-D-ribosyl-[dinitrogen reductase]
show the reaction diagram
nicotinamide guanine dinucleotide + [dinitrogen reductase]
?
show the reaction diagram
-
-
-
-
?
nicotinamide hypoxanthine dinucleotide + [dinitrogen reductase]
?
show the reaction diagram
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-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
NAD+ + [dinitrogen reductase]
?
show the reaction diagram
NAD+ + [dinitrogen reductase]
nicotinamide + ADP-D-ribosyl-[dinitrogen reductase]
show the reaction diagram
additional information
?
-
-
ADP-ribosylation of dinitrogenase reductase, NifH, occurs in response to addition of ammonium to the extracellular medium and is mediated by dinitrogenase reductase ADP-ribosyltransferase, DraT, and reversed by dinitrogenase reductase glycohydrolase, DraG, regulation, overview
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2'-deoxy-ADP
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activation
ADP
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activation
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
3-aminobenzamide
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-
KCl
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reversible
MgATP2-
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in the presence of Mg-ADP
nicotinamide
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-
additional information
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intracellular fluctuation of the PII ligands play a key role in the post-translational regulation of activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2'-deoxy-ADP
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activation
ADP-beta-S
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i.e. adenosine 5'-O-(2-thiodiphosphate), activation
MgADP-
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stimulation by binding to dinitrogen reductase (not from Azotobacter vinelandii), no activation by ATP, GDP, IDP, etheno-ADP, AMP-CH2-P, 8-bromo-ADP
protein Gln B
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regulates DraT activity. GlnB promotes a significant solubilization of HisDraT, which again suggests a possible conformational change in DraT upon GlnB binding. HisDraT has lower affinity for Ni2+ when complexed with GlnB. DraT-GlnB complex is more stable in ADP
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protein GlnB
GlnB, a nitrogen-signaling PII protein, is necessary for DraT activity in the presence of Mg-ADP
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protein GlnZ
GlnZ, a nitrogen-signaling PII protein, activates DraT activity
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additional information
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intracellular fluctuation of the PII ligands play a key role in the post-translational regulation of activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.166 - 2.5
NAD+
additional information
additional information
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activity of enzyme depends on the redox status of the Fe4S41+/2+ cluster of nitrogenase Fe protein
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.501
NAD+
Azospirillum brasilense
Q9JP48
pH 7.5, 30C, Fe protein as the acceptor of ADP-ribose, in the presence of MgADP-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.018
NAD+
Azospirillum brasilense
Q9JP48
pH 7.5, 30C, Fe protein as the acceptor of ADP-ribose, in the presence of MgADP-
7
additional information
additional information
Azospirillum brasilense
Q9JP48
the DraT-GlnB complex is at least 18fold more efficient than DraT purified from Rhodospirillum rubrum
2
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.004 - 0.015
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-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30900
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 37000, SDS-PAGE
monomer
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1 * 29000, SDS-PAGE
additional information
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chemical cross-linking of enzyme dinitrogenase reductase substrate
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ADP and NaCl stabilize during purification and storage
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bovine serum albumin increases stability towards freeze thawing in the absence of ADP
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desalting procedures during purification inactivate
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DTT stabilizes during purification
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extremely unstable in crude extract or partially purified preparation
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one freeze-thawing cycle leads to 50% loss of activity, ADP stabilizes
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, in liquid N2
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0C, in 0.2 M NaCl and 1 mM ADP, 18 h
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HisDraT-GlnB complex formed in vivo purified to homogeneity in the presence of ADP, on Ni2+ column
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recombinant His-tagged enzyme
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recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
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to near homogeneity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of the His-tagged enzyme
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functional overexpression in Escherichia coli as N-terminally His6-tagged protein, leading to NifH Fe-Protein modification in absence of ammonium, i.e. the recombinant His-tagged enzyme loses its regulation
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plasmids pLHPETDraT and pLHDK5pII co-expressed in Escherichia coli BL21
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information