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
2.4.2.37
-
RECOMMENDED NAME
GeneOntology No.
NAD+-dinitrogen-reductase ADP-D-ribosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
NAD+ + [dinitrogen reductase] = nicotinamide + ADP-D-ribosyl-[dinitrogen reductase]
show the reaction diagram
-
-
-
-
NAD+ + [dinitrogen reductase] = nicotinamide + ADP-D-ribosyl-[dinitrogen reductase]
show the reaction diagram
regulation of enzyme, signal pathways
-
NAD+ + [dinitrogen reductase] = nicotinamide + ADP-D-ribosyl-[dinitrogen reductase]
show the reaction diagram
regulation of nitrogenase by enzyme and dinitrogenase reductase activating glycohydrolase
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pentosyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
NAD+:[dinitrogen reductase] (ADP-D-ribosyl)transferase
Together with EC 3.2.2.24 (ADP-ribosyl-[dinitrogen reductase] hydrolase), controls the level of activity of EC 1.18.6.1 nitrogenase.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
(adenosine diphosphoribose)transferase, nicotinamide adenine dinucleotide-azoferredoxin
-
-
-
-
ADP-ribosyltransferase
-
-
-
-
azoferredoxin ADP-ribosyltransferase
-
-
-
-
dinitrogenase reductase ADP-ribosyltransferase
-
-
-
-
dinitrogenase reductase ADP-ribosyltransferase
-
-
dinitrogenase reductase ADP-ribosyltransferase
Q9JP48
-
dinitrogenase reductase ADP-ribosyltransferase
-
-
DRAT
-
-
-
-
NAD-azoferredoxin (ADPribose)transferase
-
-
-
-
NAD-dinitrogen-reductase ADP-D-ribosyltransferase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
117590-45-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
several strains
-
-
Manually annotated by BRENDA team
Azospirillum brasilense Sp7
strain Sp7
-
-
Manually annotated by BRENDA team
several genotypes
-
-
Manually annotated by BRENDA team
strain UR2
-
-
Manually annotated by BRENDA team
Rhodospirillum rubrum UR2
strain UR2
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
Q6N757, -
mutation of draT2 results in inactivation of the nitrogenase posttranslational modification system and in increased H2 production by ammonium-grown NifA cells
physiological function
Q6N757, -
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 ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
NAD+ + dinitrogen reductase
nicotinamide + ADP-D-ribosyl-[dinitrogen reductase]
show the reaction diagram
Q9JP48
Fe protein as the acceptor of ADP-ribose
-
-
?
NAD+ + [dinitrogen reductase]
nicotinamide + ADP-D-ribosyl-[dinitrogen reductase]
show the reaction diagram
-
-
-
-
?
NAD+ + [dinitrogen reductase]
nicotinamide + ADP-D-ribosyl-[dinitrogen reductase]
show the reaction diagram
-
-
-
-
r
NAD+ + [dinitrogen reductase]
nicotinamide + ADP-D-ribosyl-[dinitrogen reductase]
show the reaction diagram
-
-
-
-
?
NAD+ + [dinitrogen reductase]
nicotinamide + ADP-D-ribosyl-[dinitrogen reductase]
show the reaction diagram
-
high specificity for acceptor substrate, the only acceptor is dinitrogen reductase
-
?
NAD+ + [dinitrogen reductase]
nicotinamide + ADP-D-ribosyl-[dinitrogen reductase]
show the reaction diagram
-
high specificity for acceptor substrate, the only acceptor is dinitrogen reductase
-
-
?
NAD+ + [dinitrogen reductase]
nicotinamide + ADP-D-ribosyl-[dinitrogen reductase]
show the reaction diagram
-
high specificity for acceptor substrate, the only acceptor is dinitrogen reductase
-
-
?
NAD+ + [dinitrogen reductase]
nicotinamide + ADP-D-ribosyl-[dinitrogen reductase]
show the reaction diagram
-
enzyme is involved in posttranslational regulation of the nitrogenase, regulation in relation to dinitrogenase reductase-activating glycohydrolase
-
-
?
NAD+ + [dinitrogen reductase]
nicotinamide + ADP-D-ribosyl-[dinitrogen reductase]
show the reaction diagram
-
enzyme is involved in regulation of nitrogen fixation, enzyme acts together with the dinitrogenase reductase glycohydrolase DraG in posttranslational modification of the nitrogenase involving NH4Cl, overview, regulation of the enzyme, overview
-
-
r
NAD+ + [dinitrogen reductase]
nicotinamide + ADP-D-ribosyl-[dinitrogen reductase]
show the reaction diagram
Rhodospirillum rubrum UR2
-
high specificity for acceptor substrate, the only acceptor is dinitrogen reductase
-
-
?
NAD+ + [dinitrogen reductase]
nicotinamide + ADP-D-ribosyl-[dinitrogen reductase]
show the reaction diagram
Rhodospirillum rubrum UR2
-
-
-
-
?
NAD+ + [dinitrogen reductase]
nicotinamide + ADP-D-ribosyl-[dinitrogen reductase]
show the reaction diagram
Azospirillum brasilense Sp7
-
-
-
-
?
NAD+ + [dinitrogen reductase]
?
show the reaction diagram
-
involved in regulation of nitrogenase EC 1.18.6.1 through reversible ADP-ribosylation of one of the two identical subunits of dinitrogenase reductase (i.e. component II or iron protein)
-
-
?
NAD+ + [dinitrogen reductase]
?
show the reaction diagram
-
involved in regulation of nitrogenase EC 1.18.6.1 activity
-
-
?
NAD+ + [dinitrogen reductase]
?
show the reaction diagram
Rhodospirillum rubrum UR2
-
involved in regulation of nitrogenase EC 1.18.6.1 through reversible ADP-ribosylation of one of the two identical subunits of dinitrogenase reductase (i.e. component II or iron protein), involved in regulation of nitrogenase EC 1.18.6.1 activity
-
-
?
nicotinamide guanine dinucleotide + [dinitrogen reductase]
?
show the reaction diagram
-
-
-
-
?
nicotinamide hypoxanthine dinucleotide + [dinitrogen reductase]
?
show the reaction diagram
-
-
-
-
?
etheno-NAD+ + [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, DraT interacts with deuridylylated GlnB, as well as with GlnZ independently of the GlnZ uridylylation status, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
NAD+ + [dinitrogen reductase]
nicotinamide + ADP-D-ribosyl-[dinitrogen reductase]
show the reaction diagram
-
enzyme is involved in posttranslational regulation of the nitrogenase, regulation in relation to dinitrogenase reductase-activating glycohydrolase
-
-
?
NAD+ + [dinitrogen reductase]
nicotinamide + ADP-D-ribosyl-[dinitrogen reductase]
show the reaction diagram
-
enzyme is involved in regulation of nitrogen fixation, enzyme acts together with the dinitrogenase reductase glycohydrolase DraG in posttranslational modification of the nitrogenase involving NH4Cl, overview, regulation of the enzyme, overview
-
-
r
NAD+ + [dinitrogen reductase]
?
show the reaction diagram
-
involved in regulation of nitrogenase EC 1.18.6.1 through reversible ADP-ribosylation of one of the two identical subunits of dinitrogenase reductase (i.e. component II or iron protein)
-
-
?
NAD+ + [dinitrogen reductase]
?
show the reaction diagram
-
involved in regulation of nitrogenase EC 1.18.6.1 activity
-
-
?
NAD+ + [dinitrogen reductase]
?
show the reaction diagram
Rhodospirillum rubrum UR2
-
involved in regulation of nitrogenase EC 1.18.6.1 through reversible ADP-ribosylation of one of the two identical subunits of dinitrogenase reductase (i.e. component II or iron protein), involved in regulation of nitrogenase EC 1.18.6.1 activity
-
-
?
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
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2'-deoxy-ADP
-
activation
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Mg2+
-
activation
Mg2+
Q9JP48
MgADP- required. DraT-GlnB is ineffective in the presence of MgATP2-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-oxoglutarate
-
destabilizes the DraT-GlnB complex
2-oxoglutarate
Q9JP48
-
3-Aminobenzamide
-
-
ATP
-
in the presence of ADP, 63% inhibition at 1,5 mM
ATP
-
destabilizes the DraT-GlnB complex
MgATP2-
-
in the presence of Mg-ADP
additional information
-
intracellular fluctuation of the PII ligands play a key role in the post-translational regulation of activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2'-deoxy-ADP
-
activation
ADP-beta-S
-
i.e. adenosine 5'-O-(2-thiodiphosphate), activation
protein Gln B
-
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
-
protein GlnB
Q9JP48
GlnB, a nitrogen-signaling PII protein, is necessary for DraT activity in the presence of Mg-ADP
-
protein GlnZ
Q9JP48
GlnZ, a nitrogen-signaling PII protein, activates DraT activity
-
MgADP-
-
stimulation by binding to dinitrogen reductase (not from Azotobacter vinelandii), no activation by ATP, GDP, IDP, etheno-ADP, AMP-CH2-P, 8-bromo-ADP
additional information
-
intracellular fluctuation of the PII ligands play a key role in the post-translational regulation of activity
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.166
-
NAD+
Q9JP48
pH 7.5, 30C, Fe protein as the acceptor of ADP-ribose, in the presence of MgADP-
0.7
-
NAD+
-
cosubstrate ADP-D-ribosyl-[dinitrogen reductase] from Azotobacter vinelandii, in the absence of MgADP-
2
-
NAD+
-
cosubstrate native ADP-D-ribosyl-[dinitrogen reductase], in the presence of MgADP-
2.5
-
NAD+
-
cosubstrate ADP-D-ribosyl-[dinitrogen reductase] from Klebsiella pneumoniae, in the absence of MgADP-
additional information
-
additional information
-
activity of enzyme depends on the redox status of the Fe4S41+/2+ cluster of nitrogenase Fe protein
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.501
-
NAD+
Q9JP48
pH 7.5, 30C, Fe protein as the acceptor of ADP-ribose, in the presence of MgADP-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3.018
-
NAD+
Q9JP48
pH 7.5, 30C, Fe protein as the acceptor of ADP-ribose, in the presence of MgADP-
14330
additional information
-
additional information
Q9JP48
the DraT-GlnB complex is at least 18fold more efficient than DraT purified from Rhodospirillum rubrum
0
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.004
0.015
-
-
additional information
-
-
-
additional information
-
-
activity in different strains overexpressing mutants of the dinitrogenase reductase-activating glycohydrolase
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
Q9JP48
assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
Q9JP48
assay at
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30900
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 37000, SDS-PAGE
monomer
-
1 * 29000, SDS-PAGE
additional information
-
chemical cross-linking of enzyme dinitrogenase reductase substrate
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ADP and NaCl stabilize during purification and storage
-
bovine serum albumin increases stability towards freeze thawing in the absence of ADP
-
desalting procedures during purification inactivate
-
DTT stabilizes during purification
-
extremely unstable in crude extract or partially purified preparation
-
one freeze-thawing cycle leads to 50% loss of activity, ADP stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-80C, in liquid N2
-
0C, in 0.2 M NaCl and 1 mM ADP, 18 h
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
HisDraT-GlnB complex formed in vivo purified to homogeneity in the presence of ADP, on Ni2+ column
-
recombinant His-tagged enzyme
-
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
to near homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression of the His-tagged enzyme
-
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
-
plasmids pLHPETDraT and pLHDK5pII co-expressed in Escherichia coli BL21
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
enzyme mutants with altered substrate recognition and with altered posttranslational regulation of enzyme activity
additional information
-
random PCR mutagenesis, mutants with altered regulatory properties