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Information on EC 3.2.2.24 - ADP-ribosyl-[dinitrogen reductase] hydrolase
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EC Tree
3.2.2.24 ADP-ribosyl-[dinitrogen reductase] hydrolaseIUBMB Comments
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.
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Word Map
- 3.2.2.24
-
adp-ribosylation
- rhodospirillum
- rubrum
- adp-ribosyltransferase
- azospirillum
- brasilense
- adp-ribose
- pii
- macrod2
-
mono-adp-ribosylation
-
dratg
- fe-protein
- lipoferum
- glnz
-
macrodomains
-
switch-off
The enzyme appears in viruses and cellular organisms
Synonyms
dinitrogenase reductase-activating glycohydrolase, dinitrogenase reductase activating glycohydrolase, mono-adp-ribosylhydrolase, adp-ribosylglycohydrolase, dinitrogenase reductase glycohydrolase, adp-ribosyl glycohydrolase, dinitrogenase reductase adp-glycohydrolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADP-ribosyl glycohydrolase
-
-
-
-
ADP-ribosylglycohydrolase
-
-
-
-
azoferredoxin-activating enzymes
-
-
-
-
dinitrogenase reductase ADP-glycohydrolase
dinitrogenase reductase glycohydrolase
dinitrogenase reductase-activating glycohydrolase
DRAG
glycosidase, azoferredoxin
-
-
-
-
additional information
the enzyme is a member of the ADP-ribosylhydrolase family
dinitrogenase reductase-activating glycohydrolase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[dinitrogen reductase]-Nomega-alpha-(ADP-D-ribosyl)-L-arginine = ADP-D-ribose + [dinitrogen reductase]-L-arginine
[dinitrogen reductase]-Nomega-alpha-(ADP-D-ribosyl)-L-arginine = ADP-D-ribose + [dinitrogen reductase]-L-arginine
regulation of enzyme activity
-
[dinitrogen reductase]-Nomega-alpha-(ADP-D-ribosyl)-L-arginine = ADP-D-ribose + [dinitrogen reductase]-L-arginine
together with EC 2.4.2.37 NAD+-dinitrogen-reductase ADP-D-ribosyltransferase, controls the level of activity of EC 1.18.6.1 nitrogenase
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-
-
[dinitrogen reductase]-Nomega-alpha-(ADP-D-ribosyl)-L-arginine = ADP-D-ribose + [dinitrogen reductase]-L-arginine
substrate binding structure and detailed catalytic mechanism for protein de-ADP-ribosylation involving ring opening of the substrate ribose, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of N-glycosyl bond
-
-
-
-
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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.
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CAS REGISTRY NUMBER
COMMENTARY
125626-63-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ADP-D-ribosyl-(dinitrogen reductase) component of nitrogenase complex
ADP-ribose + (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
-
-
?
ADP-D-ribosyl-(dinitrogen reductase) component of nitrogenase complex + H2O
ADP-ribose + (dinitrogen reductase) component of nitrogenase complex
ADP-D-ribosyl-[dinitrogen reductase]
ADP-D-ribose + [dinitrogen reductase]
-
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
Nalpha-dansyl-Nomega-(1,N6-etheno-ADP-ribosyl)-arginine methyl ester
ADP-ribose + Nalpha-dansyl-Nomega-(1,N6-ethyl)-arginine methyl ester
-
-
-
-
?
ADP-D-ribosyl-(dinitrogen reductase) component of nitrogenase complex + H2O
ADP-ribose + (dinitrogen reductase) component of nitrogenase complex
-
-
-
-
?
ADP-D-ribosyl-(dinitrogen reductase) component of nitrogenase complex + H2O
ADP-ribose + (dinitrogen reductase) component of nitrogenase complex
-
ADP-ribosylation of initrogenase 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). The PII protein GlnZ is implicated in regulation DraG. DraG binds to both the uridylylated and deuridylylated forms of GlnZ
-
-
?
ADP-D-ribosyl-(dinitrogen reductase) component of nitrogenase complex + H2O
ADP-ribose + (dinitrogen reductase) component of nitrogenase complex
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-
-
-
?
ADP-D-ribosyl-(dinitrogen reductase) component of nitrogenase complex + H2O
ADP-ribose + (dinitrogen reductase) component of nitrogenase complex
-
nitrogenase activity in Rhodospirillum rubrum is post-translationally regulated by DRAG (dinitrogenase reductase glycohydrolase) and DRAT (dinitrogenase reductase ADP-ribosylation transferase). When a sudden increase in fixed nitrogen concentration or energy depletion is sensed by the cells, DRAG is inactivated and DRAT activated
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
i.e. component II or Fe-protein, one of the two identical subunits of dinitrogen reductase
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
i.e. component II or Fe-protein, one of the two identical subunits of dinitrogen reductase
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?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
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-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
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-
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?
ADP-ribosyl-[dinitrogen reductase] + H2O
ADP-ribose + [dinitrogen reductase]
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-
-
?
ADP-ribosyl-[dinitrogen reductase] + H2O
ADP-ribose + [dinitrogen reductase]
substrate is the Azospirillum brasilense dinitrogenase, DraG on Arg101, modeling of the binding of the substrate ADP-ribosyl moiety to DraG, active site structure, overview
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-
?
ADP-ribosyl-[dinitrogen reductase] + H2O
ADP-ribose + [dinitrogen reductase]
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-
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?
ADP-ribosyl-[dinitrogen reductase] + H2O
ADP-ribose + [dinitrogen reductase]
DraG removes ADP-ribose upon exposure of the bacteria to light or depletion of the nitrogen source added, regenerating the arginine guanidino group and activating the dinitrogenase reductase dimer
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-
?
ADP-ribosylated Fe-protein
ADP-D-ribose + Fe-protein
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-
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?
additional information
?
-
the enzyme acts specifically towards a mono-ADP-ribosylated substrate, structure-function relationship, overview
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-
?
additional information
?
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the enzyme acts specifically towards a mono-ADP-ribosylated substrate, structure-function relationship, overview
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-
?
additional information
?
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-
no substrate: dinitrogen reductase from Anabaena variabilis
-
-
?
additional information
?
-
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activity depends on oxidation state of Fe protein, with reduced Fe protein about 2% of activity compared to oxidized substrate
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-
?
additional information
?
-
DraG is capable of auto ADP-ribosylation when in excess of ADP-ribose, this reaction can function as an autoregulatory mechanism in vivo
-
-
?
additional information
?
-
-
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ADP-D-ribosyl-(dinitrogen reductase) component of nitrogenase complex + H2O
ADP-ribose + (dinitrogen reductase) component of nitrogenase complex
ADP-D-ribosyl-[dinitrogen reductase]
ADP-D-ribose + [dinitrogen reductase]
-
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
ADP-D-ribosyl-(dinitrogen reductase) component of nitrogenase complex + H2O
ADP-ribose + (dinitrogen reductase) component of nitrogenase complex
-
ADP-ribosylation of initrogenase 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). The PII protein GlnZ is implicated in regulation DraG. DraG binds to both the uridylylated and deuridylylated forms of GlnZ
-
-
?
ADP-D-ribosyl-(dinitrogen reductase) component of nitrogenase complex + H2O
ADP-ribose + (dinitrogen reductase) component of nitrogenase complex
-
nitrogenase activity in Rhodospirillum rubrum is post-translationally regulated by DRAG (dinitrogenase reductase glycohydrolase) and DRAT (dinitrogenase reductase ADP-ribosylation transferase). When a sudden increase in fixed nitrogen concentration or energy depletion is sensed by the cells, DRAG is inactivated and DRAT activated
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
i.e. component II or Fe-protein, one of the two identical subunits of dinitrogen reductase
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
i.e. component II or Fe-protein, one of the two identical subunits of dinitrogen reductase
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-D-ribosyl-[dinitrogen reductase] component of nitrogenase complex
ADPribose + [dinitrogen reductase] component of nitrogenase complex
-
-
-
?
ADP-ribosyl-[dinitrogen reductase] + H2O
ADP-ribose + [dinitrogen reductase]
-
-
-
?
ADP-ribosyl-[dinitrogen reductase] + H2O
ADP-ribose + [dinitrogen reductase]
DraG removes ADP-ribose upon exposure of the bacteria to light or depletion of the nitrogen source added, regenerating the arginine guanidino group and activating the dinitrogenase reductase dimer
-
-
?
ADP-ribosylated Fe-protein
ADP-D-ribose + Fe-protein
-
-
-
?
additional information
?
-
DraG is capable of auto ADP-ribosylation when in excess of ADP-ribose, this reaction can function as an autoregulatory mechanism in vivo
-
-
?
additional information
?
-
-
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
LITERATURE
Mn2+
additional information
-
no covalently bound inorganic cofactors, inductively coupled plasma emission analysis, detection limit for Mn2+: 0.00005 mM
Mn2+
the enzyme shows an all-alpha-helix structure with two magnesium ions located in the active site
Mn2+
two manganese ions per enzyme molecule bound at the active site, structure of the dinuclear binding site, overview. DraG shows a preference for manganese over magnesium, although not requiring a redox active metal for the reaction
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
GlnZ
the enzyme is partially inhibited by GlnZ. Enzyme inactivation requires the formation of a ternary enzyme-GlnZ-AmtB complex in vitro
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
MgGDP-
-
up to 4fold increase in activity at 10 mM due to release from chromatophore membrane
additional information
-
GTP may be involved in regulation of enzyme by controlling the extent of enzyme association with the membrane
-
additional information
-
regulation of nitrogenase activity by the enzyme/dinitrogenase reductase ADP-ribosyl transferase regulatory system in response to NH4+ and darkness requires PII protein homologs GlnB or GlnJ
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Colorectal Neoplasms
Copy Number Variation Pattern for Discriminating MACROD2 States of Colorectal Cancer Subtypes.
Colorectal Neoplasms
MACROD2 Haploinsufficiency Impairs Catalytic Activity of PARP1 and Promotes Chromosome Instability and Growth of Intestinal Tumors.
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
Mono-ADP-Ribosylhydrolase MACROD2 Is Dispensable for Murine Responses to Metabolic and Genotoxic Insults.
Intellectual Disability
Mono-ADP-Ribosylhydrolase MACROD2 Is Dispensable for Murine Responses to Metabolic and Genotoxic Insults.
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40.1
56.6
-
strain UR276, anaerobic preparation, prepared in the presence of 1 mM dithionite, pH 7.5
additional information
40.1
-
strain UR1, anaerobic preparation, prepared in the presence of 1 mM dithionite, pH 7.5
additional information
-
model in which membrane association of enzyme after an ammonium shock creates a physical separation from its cytoplasmic substrate dinitrogenase reductase thereby inhibiting ADP-ribosyl-formation. Model for control of ADP-ribosylation
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
associated to membrane of, release by treatment with MgGDP
-
brenda
-
ammonium transport protein and P11 protein are possible candidates for association with DRAG in chromatophore membranes
-
brenda
-
ammonium transport protein and P11 protein are possible candidates for association with DRAG in chromatophore membranes
-
-
brenda
-
associated to membrane after an ammonium shock
brenda
-
associated to membrane. Purified enzyme reversibly binds to bacterial pellet fractions requiring a protein component in the membrane. Guanosine and uridine tri- and di-nucleotides specifically dissociate enzyme from membrane fractions
brenda
DraG reversibly associates with the cell membrane
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
DraG is a key player in the regulation of nitrogenase activity. The enzyme, catalyzing removal of the ADP-ribose moiety, is involved in the reversible ADP-ribosylation, a ubiquitous regulatory posttranslational modification involved in numerous key processes such as DNA repair, transcription, cell differentiation, apoptosis, and the pathogenic mechanism of certain bacterial toxins
physiological function
protein-reversible ADP-ribosylation is an important posttranslational modification used to control enzymatic and protein activity in different biological systems. This modification regulates nitrogenase activity in several nitrogen-fixing bacterial species. ADP-ribosylation is catalyzed by ADP-ribosyltransferases and is reversed by ADP-ribosylhydrolases
Show AA Sequence and Transmembrane Helices (999 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
additional information
the enzyme hows an all-alpha-helix structure with two magnesium ions located in the active site. Structure comparison to the human ARH3
additional information
-
the enzyme hows an all-alpha-helix structure with two magnesium ions located in the active site. Structure comparison to the human ARH3
additional information
-
purified enzyme reversibly binds to bacterial pellet fractions, dissociation is mediated by guanosine and uridine tri- and di-nucleotides
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 35% (v/v) glycerol ethoxylate and 0.2 M lithium citrate
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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C102S
-
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
E279R
-
catalytic and electron paramagnetic resonance spectral properties like wild type
H142L
-
catalytic and electron paramagnetic resonance spectral properties like wild type
N100K
-
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
-
enzyme maintains activity after removal of light, and shows higher affinity for the calcium site of the hydroxylapatite column than wild-type
additional information
additional information
-
physiological effects of mutants lacking enzyme activity
additional information
-
overexpression of enzyme results in only partial ADP-ribosylation of Fe protein by adding ammonium. Loss of regulation after overespression may be due to titrating out negative regulators
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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
-
646967
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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
HiTrap heparin column chromatography or His-Trap column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fitzmaurice, W.P.; Saari, L.L.; Lowery, R.G.; Ludden, P.W.; Roberts, G.P.
Genes coding for the reversible ADP-ribosylation system of dinitrogenase reductase from Rhodospirillum rubrum
Mol. Gen. Genet.
218
340-347
1989
Rhodospirillum rubrum, Rhodospirillum rubrum UR2
brenda
Fu, H.A.; Fitzmaurice, W.P.; Roberts, G.P.; Burris, R.H.
Cloning and expression of draTG genes from Azospirillum lipoferum
Gene
86
95-98
1990
Azospirillum lipoferum
brenda
Fu, H.A.; Hartman, A.; Lowery, R.G.; Fitzmaurice, W.P.; Roberts, G.P.; Burris, R.H.
Posttranslational regulatory system for nitrogenase activity in Azospirillum spp
J. Bacteriol.
171
4679-4685
1989
Azospirillum brasilense, Azospirillum lipoferum, Azospirillum lipoferum SpBr17
brenda
Zhang, Y.; Burris, R.H.; Roberts, G.P.
Cloning, sequencing, mutagenesis, and functional characterization of draT and draG genes from Azospirillum brasilense
J. Bacteriol.
174
3364-3369
1992
Azospirillum brasilense, Rhodospirillum rubrum, Rhodospirillum rubrum UR2
brenda
Grunwald, S.K.; Lies, D.P.; Roberts, G.P.; Ludden, P.W.
Posttranslational regulation of nitrogenase in Rhodospirillum rubrum strains overexpressing the regulatory enzymes dinitrogenase reductase ADP-Ribosyltransferase and dinitrogenase reductase activating glycohydrolase
J. Bacteriol.
177
628-635
1995
Rhodospirillum rubrum
brenda
Zhang, Y.; Burris, R.H.; Ludden, P.W.; Roberts, G.P.
Comparison studies of dinitrogenase reductase ADP-ribosyl transferase/dinitrogenase reductase activating glycohydrolase regulatory systems in Rhodospirillum rubrum and Azospirillum brasilense
J. Bacteriol.
177
2354-2359
1995
Azospirillum brasilense, Rhodospirillum rubrum
brenda
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
J. Biol. Chem.
275
3493-3500
2000
Rhodospirillum rubrum
brenda
Zhang, Y.; Pohlmann, E.L.; Halbleib, C.M.; Ludden, P.W.; Roberts, G.P.
Effect of PII and its homolog GlnK on reversible ADP-ribosylation of dinitrogenase reductase by heterologous expression of the Rhodospirillum rubrum dinitrogenase reductase ADP-ribosyl transferase-dinitrogenase reductase-activating glycohydrolase regulatory system in Klebsiella pneumoniae
J. Bacteriol.
183
1610-1620
2001
Rhodospirillum rubrum
brenda
Saari, L.L.; Triplett, E.W.; Ludden, P.W.
Purification and properties of the activating enzyme for iron protein of nitrogenase from the photosynthetic bacterium Rhodospirillum rubrum
J. Biol. Chem.
259
15502-15508
1984
Rhodospirillum rubrum
brenda
Pope, M.R.; Saari, L.L.; Ludden, P.W.
N-glycohydrolysis of adenosine diphosphoribosyl arginine linkages by dinitrogenase reductase activating glycohydrolase (activating enzyme) from Rhodospirillum rubrum
J. Biol. Chem.
261
10104-10111
1986
Rhodospirillum rubrum
brenda
Ljungstrm, E.; Yates, M.G.; Nordlund, S.
Purification of the activating enzyme for the iron protein of nitrogenase from Azospirillum brasilense
Biochim. Biophys. Acta
994
210-214
1989
Azospirillum brasilense
-
brenda
Fu, H.; Burris, R.H.; Roberts, G.P.
Reversible ADP-ribosylation is demonstrated to be a regulatory mechanism in prokaryotes by heterologous expression
Proc. Natl. Acad. Sci. USA
87
1720-1724
1990
Azospirillum lipoferum, Rhodospirillum rubrum
brenda
Liang, J.; Nielsen, G.M.; Lies, D.P.; Burris, R.H.; Roberts, G.P.; Ludden, P.W.
Mutations in the draT and draG genes of Rhodospirillum rubrum result in loss of regulation of nitrogenase by reversible ADP-ribosylation
J. Bacteriol.
173
6903-6909
1991
Rhodospirillum rubrum, Rhodospirillum rubrum UR2
brenda
Du, C.; Reade, J.P.H.; Rogers, L.J.; Gallon, J.R.
Dinitrogenase reductase ADP-ribosyl transferase and dinitrogenase reductase activating glycohydrolase in Gloeothece
Biochem. Soc. Trans.
22
332S
1994
Gloeothece sp.
brenda
Durner, J.; Bhm, I.; Hilz, H.; Bger, P.
Posttranslational modification of nitrogenase. Differences between the purple bacterium Rhodospirillum rubrum and the cyanobacterium Anabaena variabilis
Eur. J. Biochem.
220
125-130
1994
no activity in Anabaena variabilis, Rhodospirillum rubrum
brenda
Nielsen, G.M.; Bao, Y.; Roberts, G.P.; Ludden, P.W.
Purification and characterization of an oxygen-stable form of dinitrogenase reductase-activating glycohydrolase from Rhodospirillum rubrum
Biochem. J.
302
801-806
1994
Rhodospirillum rubrum
brenda
Antharavally, B.S.; Poyner, R.R.; Zhang, Y.; Roberts, G.P.; Ludden, P.W.
Effects of specific amino acid substitutions on activities of dinitrogenase reductase-activating glycohydrolase from Rhodospirillum rubrum
J. Bacteriol.
183
5743-5746
2001
Rhodospirillum rubrum
brenda
Halbleib, C.M.; Ludden, P.W.
Characterization of the interaction of dinitrogenase reductase-activating glycohydrolase from Rhodospirillum rubrum with bacterial membranes
Arch. Microbiol.
172
51-58
1999
Rhodospirillum rubrum
brenda
Noren, A.; Nordlund, S.
Dinitrogenase reductase-activating glycohydrolase can be released from chromatophores of Rhodospirillum rubrum by treatment with MgGDP
J. Bacteriol.
179
7872-7874
1997
Rhodospirillum rubrum
brenda
Yakunin, A.F.; Fedorov, A.S.; Laurinavichene, T.V.; Glaser, V.M.; Egorov, N.S.; Tsygankov, A.A.; Zinchenko, V.V.; Hallenbeck, P.C.
Regulation of nitrogenase in the photosynthetic bacterium Rhodobacter sphaeroides containing draTG and nifHDK genes from Rhodobacter capsulatus
Can. J. Microbiol.
47
206-212
2001
no activity in Rhodobacter sphaeroides, Rhodobacter capsulatus
brenda
Huergo, L.F.; Souza, E.M.; Steffens, M.B.; Yates, M.G.; Pedrosa, F.O.; Chubatsu, L.S.
Effects of over-expression of the regulatory enzymes DraT and DraG on the ammonium-dependent post-translational regulation of nitrogenase reductase in Azospirillum brasilense
Arch. Microbiol.
183
209-217
2005
Azospirillum brasilense
brenda
Kim, K.; Zhang, Y.; Roberts, G.P.
Characterization of altered regulation variants of dinitrogenase reductase-activating glycohydrolase from Rhodospirillum rubrum
FEBS Lett.
559
84-88
2004
Rhodospirillum rubrum
brenda
Zhang, Y.; Pohlmann, E.L.; Ludden, P.W.; Roberts, G.P.
Functional characterization of three GlnB homologs in the photosynthetic bacterium Rhodospirillum rubrum: roles in sensing ammonium and energy status
J. Bacteriol.
183
6159-6168
2001
Rhodospirillum rubrum
brenda
Huergo, L.F.; Souza, E.M.; Araujo, M.S.; Pedrosa, F.O.; Chubatsu, L.S.; Steffens, M.B.; Merrick, M.
ADP-ribosylation of dinitrogenase reductase in Azospirillum brasilense is regulated by AmtB-dependent membrane sequestration of DraG
Mol. Microbiol.
59
326-337
2006
Azospirillum brasilense
brenda
Huergo, L.F.; Chubatsu, L.S.; Souza, E.M.; Pedrosa, F.O.; Steffens, M.B.; Merrick, M.
Interactions between PII proteins and the nitrogenase regulatory enzymes DraT and DraG in Azospirillum brasilense
FEBS Lett.
580
5232-5236
2006
Azospirillum brasilense
brenda
Wang, H.; Noren, A.
Metabolic regulation of nitrogen fixation in Rhodospirillum rubrum
Biochem. Soc. Trans.
34
160-161
2006
Rhodospirillum rubrum
brenda
Akentieva, N.
Formation of a cross-linking complex of dinitrogenase reductase-activating glycohydrolase (DRAG) with membrane proteins from Rhodospirillum rubrum chromatophores
Biochemistry
73
171-177
2008
Rhodospirillum rubrum, Rhodospirillum rubrum S1
brenda
Zhu, Y.; Conrad, M.C.; Zhang, Y.; Roberts, G.P.
Identification of Rhodospirillum rubrum GlnB variants that are altered in their ability to interact with different targets in response to nitrogen status signals
J. Bacteriol.
188
1866-1874
2006
Rhodospirillum rubrum
brenda
Li, X.D.; Huergo, L.F.; Gasperina, A.; Pedrosa, F.O.; Merrick, M.; Winkler, F.K.
Crystal structure of dinitrogenase reductase-activating glycohydrolase (DraG) reveals conservation in the ADP-ribosylhydrolase fold and specific features in the ADP-ribose-binding pocket
J. Mol. Biol.
390
737-746
2009
Azospirillum brasilense (A7XNI2), Azospirillum brasilense
brenda
Berthold, C.L.; Wang, H.; Nordlund, S.; Hoegbom, M.
Mechanism of ADP-ribosylation removal revealed by the structure and ligand complexes of the dimanganese mono-ADP-ribosylhydrolase DraG
Proc. Natl. Acad. Sci. USA
106
14247-14252
2009
Rhodospirillum rubrum (P14300), Rhodospirillum rubrum
brenda
Moure, V.R.; Danyal, K.; Yang, Z.Y.; Wendroth, S.; Mueller-Santos, M.; Pedrosa, F.O.; Scarduelli, M.; Gerhardt, E.C.; Huergo, L.F.; Souza, E.M.; Seefeldt, L.C.
The nitrogenase regulatory enzyme dinitrogenase reductase ADP-ribosyltransferase (DraT) is activated by direct interaction with the signal transduction protein GlnB
J. Bacteriol.
195
279-286
2013
Rhodospirillum rubrum
brenda
Nordlund, S.; Hoegbom, M.
ADP-ribosylation, a mechanism regulating nitrogenase activity
FEBS J.
280
3484-3490
2013
Rhodospirillum rubrum
brenda
Moure, V.R.; Sioeberg, C.L.B.; Valdameri, G.; Nji, E.; Oliveira, M.A.S.; Gerdhardt, E.C.M.; Pedrosa, F.O.; Mitchell, D.A.; Seefeldt, L.C.; Huergo, L.F.; Hoegbom, M.; Nordlund, S.; Souza, E.M.
The ammonium transporter AmtB and the PII signal transduction protein GlnZ are required to inhibit DraG in Azospirillum brasilense
FEBS J.
286
1214-1229
2019
Azospirillum brasilense (A7XNI2), Azospirillum brasilense FP2 (A7XNI2)
brenda
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