Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Cho, C.C.; Chien, C.Y.; Chiu, Y.C.; Lin, M.H.; Hsu, C.H.
    Structural and biochemical evidence supporting poly ADP-ribosylation in the bacterium Deinococcus radiodurans (2019), Nat. Commun., 10, 1491 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.143 recombinant expression of wild-type and mutant enzymes Deinococcus radiodurans

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.143 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

EC Number Protein Variants Comment Organism
3.2.1.143 E112A site-directed mutagenesis, inactive mutant Deinococcus radiodurans
3.2.1.143 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
3.2.1.143 T267K site-directed mutagenesis, the mutant loses its endoglycohydrolase activity but retains the exo activity on poly(ADP-ribose), PAR Deinococcus radiodurans
3.2.1.143 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.143 additional information
-
 additional information Michaelis-Menten kinetics Deinococcus radiodurans
3.2.1.143 0.00296
-
 Poly(ADP-ribose) pH 7.5, 37°C, recombinant wild-type enzyme Deinococcus radiodurans
3.2.1.143 0.00934
-
 Poly(ADP-ribose) pH 7.5, 37°C, recombinant mutant T267R Deinococcus radiodurans
3.2.1.143 0.01114
-
 Poly(ADP-ribose) pH 7.5, 37°C, recombinant mutant T267K Deinococcus radiodurans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.143 poly(ADP-ribose) + H2O Deinococcus radiodurans
-
 ?
-
 ?
3.2.1.143 poly(ADP-ribose) + H2O Deinococcus radiodurans R1
-
 ?
-
 ?
3.2.1.143 poly(ADP-ribose) + H2O Deinococcus radiodurans DSM 20539
-
 ?
-
 ?
3.2.1.143 poly(ADP-ribose) + H2O Deinococcus radiodurans VKM B-1422
-
 ?
-
 ?
3.2.1.143 poly(ADP-ribose) + H2O Deinococcus radiodurans NCIMB 9279
-
 ?
-
 ?
3.2.1.143 poly(ADP-ribose) + H2O Deinococcus radiodurans JCM 16871
-
 ?
-
 ?
3.2.1.143 poly(ADP-ribose) + H2O Deinococcus radiodurans LMG 4051
-
 ?
-
 ?
3.2.1.143 poly(ADP-ribose) + H2O Deinococcus radiodurans ATCC 13939
-
 ?
-
 ?
3.2.1.143 poly(ADP-ribose) + H2O Deinococcus radiodurans NBRC 15346
-
 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.143 Deinococcus radiodurans Q9RZM4
-
-
3.2.1.143 Deinococcus radiodurans ATCC 13939 Q9RZM4
-
-
3.2.1.143 Deinococcus radiodurans DSM 20539 Q9RZM4
-
-
3.2.1.143 Deinococcus radiodurans JCM 16871 Q9RZM4
-
-
3.2.1.143 Deinococcus radiodurans LMG 4051 Q9RZM4
-
-
3.2.1.143 Deinococcus radiodurans NBRC 15346 Q9RZM4
-
-
3.2.1.143 Deinococcus radiodurans NCIMB 9279 Q9RZM4
-
-
3.2.1.143 Deinococcus radiodurans R1 Q9RZM4
-
-
3.2.1.143 Deinococcus radiodurans VKM B-1422 Q9RZM4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.143 recombinant wild-type and mutant enzymes Deinococcus radiodurans

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.143 (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
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.143 additional information enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes Deinococcus radiodurans ?
-
 ?
3.2.1.143 additional information enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes Deinococcus radiodurans R1 ?
-
 ?
3.2.1.143 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 ?
-
 ?
3.2.1.143 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 ?
-
 ?
3.2.1.143 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 ?
-
 ?
3.2.1.143 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 ?
-
 ?
3.2.1.143 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 ?
-
 ?
3.2.1.143 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 ?
-
 ?
3.2.1.143 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 ?
-
 ?
3.2.1.143 poly(ADP-ribose) + H2O
-
 Deinococcus radiodurans ?
-
 ?
3.2.1.143 poly(ADP-ribose) + H2O enzyme-substrate binding complex structure analysis, overview Deinococcus radiodurans ?
-
 ?
3.2.1.143 poly(ADP-ribose) + H2O
-
 Deinococcus radiodurans R1 ?
-
 ?
3.2.1.143 poly(ADP-ribose) + H2O enzyme-substrate binding complex structure analysis, overview Deinococcus radiodurans R1 ?
-
 ?
3.2.1.143 poly(ADP-ribose) + H2O
-
 Deinococcus radiodurans DSM 20539 ?
-
 ?
3.2.1.143 poly(ADP-ribose) + H2O enzyme-substrate binding complex structure analysis, overview Deinococcus radiodurans DSM 20539 ?
-
 ?
3.2.1.143 poly(ADP-ribose) + H2O
-
 Deinococcus radiodurans VKM B-1422 ?
-
 ?
3.2.1.143 poly(ADP-ribose) + H2O enzyme-substrate binding complex structure analysis, overview Deinococcus radiodurans VKM B-1422 ?
-
 ?
3.2.1.143 poly(ADP-ribose) + H2O
-
 Deinococcus radiodurans NCIMB 9279 ?
-
 ?
3.2.1.143 poly(ADP-ribose) + H2O enzyme-substrate binding complex structure analysis, overview Deinococcus radiodurans NCIMB 9279 ?
-
 ?
3.2.1.143 poly(ADP-ribose) + H2O
-
 Deinococcus radiodurans JCM 16871 ?
-
 ?
3.2.1.143 poly(ADP-ribose) + H2O enzyme-substrate binding complex structure analysis, overview Deinococcus radiodurans JCM 16871 ?
-
 ?
3.2.1.143 poly(ADP-ribose) + H2O
-
 Deinococcus radiodurans LMG 4051 ?
-
 ?
3.2.1.143 poly(ADP-ribose) + H2O enzyme-substrate binding complex structure analysis, overview Deinococcus radiodurans LMG 4051 ?
-
 ?
3.2.1.143 poly(ADP-ribose) + H2O
-
 Deinococcus radiodurans ATCC 13939 ?
-
 ?
3.2.1.143 poly(ADP-ribose) + H2O enzyme-substrate binding complex structure analysis, overview Deinococcus radiodurans ATCC 13939 ?
-
 ?
3.2.1.143 poly(ADP-ribose) + H2O
-
 Deinococcus radiodurans NBRC 15346 ?
-
 ?
3.2.1.143 poly(ADP-ribose) + H2O enzyme-substrate binding complex structure analysis, overview Deinococcus radiodurans NBRC 15346 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.143 DrPARG
-
 Deinococcus radiodurans
3.2.1.143 PARG
-
 Deinococcus radiodurans
3.2.1.143 poly(ADP-ribose)glycohydrolase
-
 Deinococcus radiodurans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.143 37
-
 assay at Deinococcus radiodurans

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.143 181.4
-
 Poly(ADP-ribose) pH 7.5, 37°C, recombinant mutant T267K Deinococcus radiodurans
3.2.1.143 198.6
-
 Poly(ADP-ribose) pH 7.5, 37°C, recombinant mutant T267R Deinococcus radiodurans
3.2.1.143 266.4
-
 Poly(ADP-ribose) pH 7.5, 37°C, recombinant wild-type enzyme Deinococcus radiodurans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.143 7.5
-
 assay at Deinococcus radiodurans

Expression

EC Number Organism Comment Expression
3.2.1.143 Deinococcus radiodurans in the radio-resistant bacterium Deinococcus radiodurans, the PARG homologue, DrPARG, expression is upregulated after radiation damage up

General Information

EC Number General Information Comment Organism
3.2.1.143 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
3.2.1.143 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 [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.2.1.143 16284
-
 Poly(ADP-ribose) pH 7.5, 37°C, recombinant mutant T267K Deinococcus radiodurans
3.2.1.143 21263
-
 Poly(ADP-ribose) pH 7.5, 37°C, recombinant mutant T267R Deinococcus radiodurans
3.2.1.143 90000
-
 Poly(ADP-ribose) pH 7.5, 37°C, recombinant wild-type enzyme Deinococcus radiodurans