Information on EC 3.2.2.24 - ADP-ribosyl-[dinitrogen reductase] hydrolase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.2.2.24
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RECOMMENDED NAME
GeneOntology No.
ADP-ribosyl-[dinitrogen reductase] hydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[dinitrogen reductase]-Nomega-alpha-(ADP-D-ribosyl)-L-arginine = ADP-D-ribose + [dinitrogen reductase]-L-arginine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of N-glycosyl bond
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-
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SYSTEMATIC NAME
IUBMB Comments
ADP-D-ribosyl-[dinitrogen reductase] ADP-ribosylhydrolase
The enzyme restores the activity of EC 1.18.6.1, nitrogenase, by catalysing the removal of ADP-ribose from an arginine residue of the dinitrogenase reductase component of nitrogenase. This activity occurs only when the nitrogenase product, ammonium, is not available. The combined activity of this enzyme and EC 2.4.2.37, NAD+-dinitrogen-reductase ADP-D-ribosyltransferase, controls the level of activity of nitrogenase.
CAS REGISTRY NUMBER
COMMENTARY hide
125626-63-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cyanobacterium
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Manually annotated by BRENDA team
no activity in Anabaena variabilis
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Manually annotated by BRENDA team
no activity in Rhodobacter sphaeroides
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Manually annotated by BRENDA team
strain S1
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Manually annotated by BRENDA team
wild-type (UR2)
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP-D-ribosyl-(dinitrogen reductase) component of nitrogenase complex
ADP-ribose + (dinitrogen reductase) component of nitrogenase complex
show the reaction diagram
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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
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-
?
ADP-D-ribosyl-(dinitrogen reductase) component of nitrogenase complex + H2O
ADP-ribose + (dinitrogen reductase) component of nitrogenase complex
show the reaction diagram
ADP-D-ribosyl-[dinitrogen reductase]
ADP-D-ribose + [dinitrogen reductase]
show the reaction diagram
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-
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-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
show the reaction diagram
ADP-ribosyl-[dinitrogen reductase] + H2O
ADP-ribose + [dinitrogen reductase]
show the reaction diagram
Nalpha-dansyl-Nomega-(1,N6-etheno-ADP-ribosyl)-arginine methyl ester
ADP-ribose + Nalpha-dansyl-Nomega-(1,N6-ethyl)-arginine methyl ester
show the reaction diagram
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-
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additional information
?
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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
ADP-D-ribosyl-(dinitrogen reductase) component of nitrogenase complex + H2O
ADP-ribose + (dinitrogen reductase) component of nitrogenase complex
show the reaction diagram
ADP-D-ribosyl-[dinitrogen reductase]
ADP-D-ribose + [dinitrogen reductase]
show the reaction diagram
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-
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-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
show the reaction diagram
ADP-ribosyl-[dinitrogen reductase] + H2O
ADP-ribose + [dinitrogen reductase]
show the reaction diagram
additional information
?
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P14300
DraG is capable of auto ADP-ribosylation when in excess of ADP-ribose, this reaction can function as an autoregulatory mechanism in vivo
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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no covalently bound inorganic cofactors, inductively coupled plasma emission analysis, detection limit for Mn2+: 0.00005 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Dithionite
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in air, inactivation
H2O2
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inactivation, to the same extent as dithionite in air
additional information
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no inhibition by ADP
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
MgGDP-
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up to 4fold increase in activity at 10 mM due to release from chromatophore membrane
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.01664 - 2.055
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different strains
56.6
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strain UR276, anaerobic preparation, prepared in the presence of 1 mM dithionite, pH 7.5
138
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strain UR276, anaerobic preparation, pH 7.5
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.9 - 8.2
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about half-maximal activity at pH 6.9 and pH 8.2
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
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1 * 32000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant DraG bound to substrate Azospirillum brasilense dinitrogenase, mixing of protein solution with reservoir solution, containing 0.1M HEPES, pH 7.5, 15% w/v PEG 20000, in a 1:1 ratio,2-3 days X-ray diffraction structure determination and analysis at 2.5 resolution, modelling
purified recombinant DraG in the holo and ADP-ribose bound forms and a reaction intermediate analogue, sitting drop vapor diffusion method, 0.0006 ml of of 10 mg/ml wild-type DraG is mixed with an equal volume of 15% PEG 3350, 0.3 M NH4Cl, and 0.1 M Tris, pH 7.0, several days, cryoprotection in 20% PEG 3350, 0.3 M NH4Cl, 0.1M Tris, pH 7.0, and 20% glycerol, X-ray diffraction structure determination and analysis at 2.2 A resolution, modelling, overview
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Mn2+ renders the enzyme more susceptible to inactivation by dithionite in air, not Ca2+, Fe2+ or Mg2+, ADPribose protects, not ADP
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
attempts to purify the enzyme using aerobic buffer are partly successful, aerobic DEAE-cellulose chromatography results in rapid loss of activity, 30 min stable to exposure to air in buffer containing DTT in the absence of dithionite, in its presence decrease of activity with time, bovine serum albumin does not protect
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646967
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, purified preparation exposed to air in the absence of dithionite, 22 h
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant DraG from Escherichia coli strain BL21(DE3)
recombinant enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DraG, expression in Escherichia coli strain BL21(DE3)
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C102S
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enzyme maintains activity after removal of light, shows a significantly poorer affinity for Mn2+, and higher affinity for the calcium site of the hydroxylapatite column than wild-type
D123A
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reduced catalytic activity and binding of Mn2+
D243G
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no catalytic activity or binding of Mn2+
E279R
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catalytic and electron paramagnetic resonance spectral properties like wild type
H142L
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catalytic and electron paramagnetic resonance spectral properties like wild type
H158N
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no catalytic activity or binding of Mn2+
N100K
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enzyme maintains activity after removal of light and does not respond to addition of NH4Cl, shows a significantly poorer affinity for Mn2+ and higher affinity for the calcium site of the hydroxylapatite column than wild-type
V98L
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enzyme maintains activity after removal of light, and shows higher affinity for the calcium site of the hydroxylapatite column than wild-type
additional information
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