Cloned (Comment) | Organism |
---|---|
recombinant expression of wild-type and mutant enzymes | Deinococcus radiodurans |
Crystallization (Comment) | Organism |
---|---|
crystallization of ADP-ribose bound wild-type enzyme and mutant enzymes T267K and T267R, X-ray diffraction structure determination and analysis at 1.97 A resolution, monoclinic crystals with space group P21 | Deinococcus radiodurans |
Protein Variants | Comment | Organism |
---|---|---|
E112A | site-directed mutagenesis, inactive mutant | Deinococcus radiodurans |
additional information | disruption of DrPARG expression causes accumulation of endogenous poly-ADP-ribose (PAR) and compromises recovery from UV radiation damage. A substitution of Arg268 for the smaller and uncharged side chain of Thr267 than that of arginine disrupts the interaction matrix of Thr267, Asp260, and n ribose' and allows for accommodating the n+1 ADP-ribose | Deinococcus radiodurans |
T267K | site-directed mutagenesis, the mutant loses its endoglycohydrolase activity but retains the exo activity on poly(ADP-ribose), PAR | Deinococcus radiodurans |
T267R | site-directed mutagenesis, the mutant loses its endoglycohydrolase activity but retains the exo activity on poly(ADP-ribose), PAR | Deinococcus radiodurans |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten kinetics | Deinococcus radiodurans | |
0.00296 | - |
Poly(ADP-ribose) | pH 7.5, 37°C, recombinant wild-type enzyme | Deinococcus radiodurans | |
0.00934 | - |
Poly(ADP-ribose) | pH 7.5, 37°C, recombinant mutant T267R | Deinococcus radiodurans | |
0.01114 | - |
Poly(ADP-ribose) | pH 7.5, 37°C, recombinant mutant T267K | Deinococcus radiodurans |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
poly(ADP-ribose) + H2O | Deinococcus radiodurans | - |
? | - |
? | |
poly(ADP-ribose) + H2O | Deinococcus radiodurans R1 | - |
? | - |
? | |
poly(ADP-ribose) + H2O | Deinococcus radiodurans DSM 20539 | - |
? | - |
? | |
poly(ADP-ribose) + H2O | Deinococcus radiodurans VKM B-1422 | - |
? | - |
? | |
poly(ADP-ribose) + H2O | Deinococcus radiodurans NCIMB 9279 | - |
? | - |
? | |
poly(ADP-ribose) + H2O | Deinococcus radiodurans JCM 16871 | - |
? | - |
? | |
poly(ADP-ribose) + H2O | Deinococcus radiodurans LMG 4051 | - |
? | - |
? | |
poly(ADP-ribose) + H2O | Deinococcus radiodurans ATCC 13939 | - |
? | - |
? | |
poly(ADP-ribose) + H2O | Deinococcus radiodurans NBRC 15346 | - |
? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Deinococcus radiodurans | Q9RZM4 | - |
- |
Deinococcus radiodurans ATCC 13939 | Q9RZM4 | - |
- |
Deinococcus radiodurans DSM 20539 | Q9RZM4 | - |
- |
Deinococcus radiodurans JCM 16871 | Q9RZM4 | - |
- |
Deinococcus radiodurans LMG 4051 | Q9RZM4 | - |
- |
Deinococcus radiodurans NBRC 15346 | Q9RZM4 | - |
- |
Deinococcus radiodurans NCIMB 9279 | Q9RZM4 | - |
- |
Deinococcus radiodurans R1 | Q9RZM4 | - |
- |
Deinococcus radiodurans VKM B-1422 | Q9RZM4 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and mutant enzymes | Deinococcus radiodurans |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
(ADP-ribose)n + H2O = (ADP-ribose)n-1 + ADP-ribose | enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes | Deinococcus radiodurans |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes | Deinococcus radiodurans | ? | - |
? | |
additional information | enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes | Deinococcus radiodurans R1 | ? | - |
? | |
additional information | enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes | Deinococcus radiodurans DSM 20539 | ? | - |
? | |
additional information | enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes | Deinococcus radiodurans VKM B-1422 | ? | - |
? | |
additional information | enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes | Deinococcus radiodurans NCIMB 9279 | ? | - |
? | |
additional information | enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes | Deinococcus radiodurans JCM 16871 | ? | - |
? | |
additional information | enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes | Deinococcus radiodurans LMG 4051 | ? | - |
? | |
additional information | enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes | Deinococcus radiodurans ATCC 13939 | ? | - |
? | |
additional information | enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes | Deinococcus radiodurans NBRC 15346 | ? | - |
? | |
poly(ADP-ribose) + H2O | - |
Deinococcus radiodurans | ? | - |
? | |
poly(ADP-ribose) + H2O | enzyme-substrate binding complex structure analysis, overview | Deinococcus radiodurans | ? | - |
? | |
poly(ADP-ribose) + H2O | - |
Deinococcus radiodurans R1 | ? | - |
? | |
poly(ADP-ribose) + H2O | enzyme-substrate binding complex structure analysis, overview | Deinococcus radiodurans R1 | ? | - |
? | |
poly(ADP-ribose) + H2O | - |
Deinococcus radiodurans DSM 20539 | ? | - |
? | |
poly(ADP-ribose) + H2O | enzyme-substrate binding complex structure analysis, overview | Deinococcus radiodurans DSM 20539 | ? | - |
? | |
poly(ADP-ribose) + H2O | - |
Deinococcus radiodurans VKM B-1422 | ? | - |
? | |
poly(ADP-ribose) + H2O | enzyme-substrate binding complex structure analysis, overview | Deinococcus radiodurans VKM B-1422 | ? | - |
? | |
poly(ADP-ribose) + H2O | - |
Deinococcus radiodurans NCIMB 9279 | ? | - |
? | |
poly(ADP-ribose) + H2O | enzyme-substrate binding complex structure analysis, overview | Deinococcus radiodurans NCIMB 9279 | ? | - |
? | |
poly(ADP-ribose) + H2O | - |
Deinococcus radiodurans JCM 16871 | ? | - |
? | |
poly(ADP-ribose) + H2O | enzyme-substrate binding complex structure analysis, overview | Deinococcus radiodurans JCM 16871 | ? | - |
? | |
poly(ADP-ribose) + H2O | - |
Deinococcus radiodurans LMG 4051 | ? | - |
? | |
poly(ADP-ribose) + H2O | enzyme-substrate binding complex structure analysis, overview | Deinococcus radiodurans LMG 4051 | ? | - |
? | |
poly(ADP-ribose) + H2O | - |
Deinococcus radiodurans ATCC 13939 | ? | - |
? | |
poly(ADP-ribose) + H2O | enzyme-substrate binding complex structure analysis, overview | Deinococcus radiodurans ATCC 13939 | ? | - |
? | |
poly(ADP-ribose) + H2O | - |
Deinococcus radiodurans NBRC 15346 | ? | - |
? | |
poly(ADP-ribose) + H2O | enzyme-substrate binding complex structure analysis, overview | Deinococcus radiodurans NBRC 15346 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
DrPARG | - |
Deinococcus radiodurans |
PARG | - |
Deinococcus radiodurans |
poly(ADP-ribose)glycohydrolase | - |
Deinococcus radiodurans |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Deinococcus radiodurans |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
181.4 | - |
Poly(ADP-ribose) | pH 7.5, 37°C, recombinant mutant T267K | Deinococcus radiodurans | |
198.6 | - |
Poly(ADP-ribose) | pH 7.5, 37°C, recombinant mutant T267R | Deinococcus radiodurans | |
266.4 | - |
Poly(ADP-ribose) | pH 7.5, 37°C, recombinant wild-type enzyme | Deinococcus radiodurans |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Deinococcus radiodurans |
Organism | Comment | Expression |
---|---|---|
Deinococcus radiodurans | in the radio-resistant bacterium Deinococcus radiodurans, the PARG homologue, DrPARG, expression is upregulated after radiation damage | up |
General Information | Comment | Organism |
---|---|---|
malfunction | disruption of DrPARG expression causes accumulation of endogenous poly-ADP-ribose (PAR) and compromises recovery from UV radiation damage. Endogenous PAR levels in Deinococcus radiodurans are elevated after UV irradiation, indicating that the prokaryotic PARylation may be involved in resistance to genotoxic stresses | Deinococcus radiodurans |
additional information | CD spectra of enzyme DrPARG in the absence and presence of ADP-ribose exhibit increased proportion of alpha-helices and beta-strands from 11.78% and 30.37% to 15.10% and 33.52%, respectively, which suggests that conformational changes occur during the binding of ADP-ribose. The intrinsically disordered N-terminal region of DrPARG might be highly flexible. ADP-ribose binding pocket and complex structure, and conformational effects, detailed overview | Deinococcus radiodurans |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
16284 | - |
Poly(ADP-ribose) | pH 7.5, 37°C, recombinant mutant T267K | Deinococcus radiodurans | |
21263 | - |
Poly(ADP-ribose) | pH 7.5, 37°C, recombinant mutant T267R | Deinococcus radiodurans | |
90000 | - |
Poly(ADP-ribose) | pH 7.5, 37°C, recombinant wild-type enzyme | Deinococcus radiodurans |