3.6.1.13: ADP-ribose diphosphatase
This is an abbreviated version!
For detailed information about ADP-ribose diphosphatase, go to the full flat file.
Word Map on EC 3.6.1.13
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3.6.1.13
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pyrophosphatases
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melastatin
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mutt-related
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ribose-5'-phosphate
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adp-sugars
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8-oxo-dgdp
- 3.6.1.13
- pyrophosphatases
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melastatin
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mutt-related
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ribose-5'-phosphate
- adp-sugars
- 8-oxo-dgdp
Reaction
Synonyms
adenosine 5'-diphosphosugar pyrophosphatase, adenosine diphosphoribose pyrophosphatase, ADP-ribose diphosphatase, ADP-ribose hydrolase, ADP-ribose phosphohydrolase, ADP-ribose pyrophosphatase, ADP-ribose pyrophosphatase Sll1054, ADP-ribose pyrophosphatase Slr0920, ADP-ribose pyrophosphatase Slr1134, ADP-ribose pyrophosphatase-I, ADP-ribose/CDP-alcohol diphosphatase, ADP-ribose/NADH pyrophosphohydrolase, ADPR pyrophosphatase, ADPR-PPase, ADPRase, ADPRase-I, ADPRibase, ADPRibase-Mn, ADPribose pyrophosphatase, Adprm, AT4G12720, AtNUDT10, AtNUDT2, AtNUDT6, AtNUDT7, AtNUDX7, cADPR phosphohydrolase, CinA, cyclic ADPR phosphohydrolase, DR2204, EcADPRase, mNUDT5 protein, More, MT1739, MtADPRase, MutT/nudix family protein, NadM-Nudix, Ndx2, Ndx4, NMN adenylyltransferase/ADP-ribose pyrophosphatase, Nudix hydrolase, Nudix hydrolase 7, NUDT5, NUDT5 protein, NUDT9, NUDT9 protein, NUDT9alpha protein, NUDX2, NUDX7, NuhA, pyrophosphatase, adenosine diphosphoribose, submicromolar-K(m) ADP-ribose pyrophosphatase, TtADPRase, YSA1H, zgc:64213
ECTree
3.6.1.13 ADP-ribose diphosphataseAdvanced search results
results (
results (Engineering
Engineering on EC 3.6.1.13 - ADP-ribose diphosphatase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
H97A
mutant shows 60fold decrease in activity for substrates ADP-ribose and ADP and 300500fold for CDP-alcohols. For H97A, 2',3'-cAMP is a better substrate than ADP-ribose
C139A
C253A
mutant displays a tenfold increased efficiency for cADP-ribose, with no or modest effect on the other substrates
D133A
D133N
D164A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
D164N
the mutant shows increased catalytic efficiency compared to the wild type enzyme
E112Q
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
E115Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E116Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E166Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E93Q
F210A
lowers 40-70fold the catalytic efficiency for ADP-ribose, CDP-choline and 2',3'-cAMP hydrolysis, and 500fold for cADP-ribose
F37A
19fold increased Km for ADP-ribose, with only a 2-3fold increase of the CDP-choline and 2',3'-cAMP Km values
F37A/L196A
mutation lessens the relative preference for ADP-ribose versus cADP-ribose
F37A/L196F
mutation lessens the relative preference for ADP-ribose versus cADP-ribose
F37A/L196F/C253A
F37A/L196F/C253G
site-directed mutagenesis, the mutant with a smaller residue 253 shows increased cADPR specificity
F37A/L196F/D250A/C253G
site-directed mutagenesis, the quadruple mutant shows a detrimental effect of the D250A substitution on the efficiency with all substrates (1.3-3.4fold decrease), and more markedly so for cADPR, such that the substrate efficiency ratios are less favourable than for the triple mutant F37A/L196F/C253G
F37A/L196F/V252A/C253G
site-directed mutagenesis, the mutant with displays the desired specificity, with cADPR kcat/KM is about 20-200fold larger than for any other substrate. The quadruple mutant shows detrimental effects of the V252A substitution on the efficiency with ADP-ribose, CDP-choline and 2',3'-cAMP (1.1-2.8fold decrease) while it increases 2fold the efficiency with cADPR
L196A
mutation causes only a modest 2-5fold decrease of catalytic efficiency with the four substrates tested
L98A
N110A
100-250fold reduction in catalytic efficiency for the hydrolysis of CDP-choline or 2',3'-cAMP
Q27H
mutation reduces 11-13-fold the catalytic efficiency of the hydrolysis of ADP-ribose, CDP-choline or 2',3'-cAMP, and 27fold the hydrolysis of cADP-ribose
Q82A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
R111Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
R196Q
R51Q
R84Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
W28A
W28A/W46A
W46A
D126N
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the ratio of turnover-number to Km-value with ADPribose as substrate and Mg2+ as activator is 40% of the of the wild-type enzyme
D128N
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the ratio of turnover-number to Km-value with ADPribose as substrate and Mg2+ as activator is 74% of the of the wild-type enzyme
E127Q
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the ratio of turnover-number to Km-value with ADPribose as substrate and Mg2+ as activator is 114% of the of the wild-type enzyme
E129Q
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the ratio of turnover-number to Km-value with ADPribose as substrate and Mg2+ as activator is 32% of the of the wild-type enzyme
E82Q
E86Q
D126N
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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the ratio of turnover-number to Km-value with ADPribose as substrate and Mg2+ as activator is 40% of the of the wild-type enzyme
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D128N
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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the ratio of turnover-number to Km-value with ADPribose as substrate and Mg2+ as activator is 74% of the of the wild-type enzyme
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E127Q
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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the ratio of turnover-number to Km-value with ADPribose as substrate and Mg2+ as activator is 114% of the of the wild-type enzyme
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E129Q
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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the ratio of turnover-number to Km-value with ADPribose as substrate and Mg2+ as activator is 32% of the of the wild-type enzyme
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E86Q
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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the ratio of turnover-number to Km-value with ADPribose as substrate and Mg2+ as activator is 0.0034% of the of the wild-type enzyme
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additional information
C139A
site-directed mutagenesis, mutation causes a 2.1fold increase in Km for ADP-ribose but has no effect on kcat compared to the wild-type enzyme
C139A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
D133A
site-directed mutagenesis, mutation causes a 4.0fold increase in Km for ADP-ribose but has no effect on kcat compared to the wild-type enzyme
D133A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
D133N
site-directed mutagenesis, mutation causes a 2.1fold increase in Km for ADP-ribose but has no effect on kcat compared to the wild-type enzyme
D133N
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E93Q
site-directed mutagenesis, mutation causes a 1.8fold increase in Km for ADP-ribose but has no effect on kcat compared to the wild-type enzyme
E93Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
F37A/L196F/C253A
site-directed mutagenesis, specific cyclic ADP-ribose phosphohydrolase obtained by mutagenic engineering of Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase. Mutagenesis of human ADPRibase-Mn at Phe37, Leu196 and Cys253 alters its specificity, the best substrate of the mutant is cyclic ADP-ribose (cADPR), the Cys253 mutation is essential for cADPR preference. The proximity to the northern ribose of cADPR in docking models indicates Cys253 is a steric constraint for cADPR positioning
L98A
site-directed mutagenesis, mutation of Leu98 to Ala causes a 5.8fold increase in Km but has no effect on kcat compared to the wild-type enzyme
L98A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
R196Q
site-directed mutagenesis, mutation causes a 5.5fold increase in Km for ADP-ribose but has no effect on kcat compared to the wild-type enzyme
R196Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
R51Q
site-directed mutagenesis, the mutant shows a 14.6fold increased Km and a 17fold decreased kcat for ADP-ribose compared to the wild-type enzyme
R51Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
W28A
site-directed mutagenesis, the mutant shows 8.4fold increased Km for ADP-ribose, but unaltered kcat compared to the wild-type enzyme
W28A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
W28A/W46A
site-directed mutagenesis, the mutant shows 53.7fold increased Km and a 219fold decreased kcat for ADP-ribose compared to the wild-type enzyme
W28A/W46A
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
W46A
site-directed mutagenesis, the mutant shows 5.7fold increased Km for ADP-ribose, but unaltered kcat compared to the wild-type enzyme
W46A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E82Q
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the ratio of turnover-number to Km-value with ADPribose as substrate and Mg2+ as activator is 0.0006% of the of the wild-type enzyme
E86Q
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the ratio of turnover-number to Km-value with ADPribose as substrate and Mg2+ as activator is 0.0034% of the of the wild-type enzyme
additional information
overexpression of AtNUDX7 in Arabidopsis thaliana improves seed parameters, accelerates flowering, and reduces inflorescence height. AtNUDX7 overexpression in Arabixaddopsis might enhance the ADP-ribose recycling step and maintain energy levels by supplying an ATP source in the poly(ADP-ribosyl)ation energy homeostasis pathway. Arabidopsis and maize lines with high, medium and low overexpression levels of the AtNUDX7 gene are analysed in automated platforms and the inhibition of several growth parameters is determined under mild drought stress conditions. The constitutive overexpression of the Arabidopxadsis AtNUDX7 gene in Arabidopsis and maize at varying levels does not improve tolerance to mild drought stress, but knocking down AtNUDX7 expression does, however at the expense of general growth under normal conditions. A loss-of-function mutant line, designated Atnudx7-1 (SALK-046441), has a T-DNA insertion in exon 1 of the AtNUDX7 gene, in the Col-0 background and verified for its T-DNA insertion position, homozygous T-DNA insertion, AtNUDX7 gene expression, and is used as a negative control. Evaluation of the AtNUDX7 overexpression maize lines under mild drought stress
additional information
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overexpression of AtNUDX7 in Arabidopsis thaliana improves seed parameters, accelerates flowering, and reduces inflorescence height. AtNUDX7 overexpression in Arabixaddopsis might enhance the ADP-ribose recycling step and maintain energy levels by supplying an ATP source in the poly(ADP-ribosyl)ation energy homeostasis pathway. Arabidopsis and maize lines with high, medium and low overexpression levels of the AtNUDX7 gene are analysed in automated platforms and the inhibition of several growth parameters is determined under mild drought stress conditions. The constitutive overexpression of the Arabidopxadsis AtNUDX7 gene in Arabidopsis and maize at varying levels does not improve tolerance to mild drought stress, but knocking down AtNUDX7 expression does, however at the expense of general growth under normal conditions. A loss-of-function mutant line, designated Atnudx7-1 (SALK-046441), has a T-DNA insertion in exon 1 of the AtNUDX7 gene, in the Col-0 background and verified for its T-DNA insertion position, homozygous T-DNA insertion, AtNUDX7 gene expression, and is used as a negative control. Evaluation of the AtNUDX7 overexpression maize lines under mild drought stress
additional information
-
overexpression of AtNUDX7 in Arabidopsis thaliana improves seed parameters, accelerates flowering, and reduces inflorescence height. AtNUDX7 overexpression in Arabixaddopsis might enhance the ADP-ribose recycling step and maintain energy levels by supplying an ATP source in the poly(ADP-ribosyl)ation energy homeostasis pathway. Arabidopsis and maize lines with high, medium and low overexpression levels of the AtNUDX7 gene are analysed in automated platforms and the inhibition of several growth parameters is determined under mild drought stress conditions. The constitutive overexpression of the Arabidopxadsis AtNUDX7 gene in Arabidopsis and maize at varying levels does not improve tolerance to mild drought stress, but knocking down AtNUDX7 expression does, however at the expense of general growth under normal conditions. A loss-of-function mutant line, designated Atnudx7-1 (SALK-046441), has a T-DNA insertion in exon 1 of the AtNUDX7 gene, in the Col-0 background and verified for its T-DNA insertion position, homozygous T-DNA insertion, AtNUDX7 gene expression, and is used as a negative control. Evaluation of the AtNUDX7 overexpression maize lines under mild drought stress
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additional information
design of mutations at or near residue 253 of human ADPRibase-Mn, in the vicinity of the adenine N1-linked (northern) ribose of cADPR, for altering the substrate specificity of the enzyme, overview
