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Information on EC 3.6.1.13 - ADP-ribose diphosphatase and Organism(s) Homo sapiens
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3.6.1.13 ADP-ribose diphosphataseSpecify your search results
Word Map
- 3.6.1.13
- pyrophosphatases
-
melastatin
-
mutt-related
-
ribose-5'-phosphate
- adp-sugars
- 8-oxo-dgdp
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
nudt5, nudt9, adp-ribose pyrophosphatase, adprase, atnudt7, adpribase-mn, atnudx7, adp-ribose hydrolase, nudt5 protein, adpr pyrophosphatase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosine diphosphoribose pyrophosphatase
-
-
-
-
ADP-ribose diphosphatase
-
-
-
-
ADP-ribose phosphohydrolase
-
-
-
-
ADP-ribose pyrophosphatase
ADPR-PPase
-
-
-
-
ADPRase
ADPRibase
-
-
-
-
ADPribose pyrophosphatase
-
-
-
-
NUDT5
pyrophosphatase, adenosine diphosphoribose
-
-
-
-
additional information
ADP-ribose pyrophosphatase
-
-
-
-
additional information
-
the enzyme is a member of a superfamily of Nudix hydrolases
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate
molecular catalytic mechanism involving Arg51, Arg111, Glu112, and Glu116, active site structure, substrate binding involving Arg51, Leu98, Trp28 and Trp46 and transition-state structure, structure-function relationship, and kinetic analysis
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphorous acid anhydride hydrolysis
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ADP-D-ribose ribophosphohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY
9024-83-3
-
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
1,Nepsilon-etheno-ADP-ribose + H2O
1,Nepsilon-etheno-AMP-ribose + phosphate
-
fluorogenic substrate
the product is converted to fluorescent 1,Nepsilon-etheno-adenosine by alkaline phosphatase for detection
-
?
CDP-glucose + H2O
CMP + glucose 5-phosphate
-
at 5% of the activity with ADPribose
-
-
?
diadenosine 5',5''-diphosphate + H2O
?
20% the activity with ADP-ribose
-
-
?
IDP-ribose + H2O
IMP + D-ribose 5-phosphate
-
138% of the activity with ADPribose
-
-
?
IDPribose + H2O
IMP + D-ribose 5-phosphate
77% of the activity with ADPribose
-
-
?
UDP-galactose + H2O
UDP + galactose
7% of the activity with ADP-ribose
-
-
?
ADP-glucose + H2O
AMP + alpha-D-glucose 1-phosphate
-
at 21% of the activity with ADPribose
-
-
?
ADP-glucose + H2O
AMP + alpha-D-glucose 1-phosphate
56% of the activity with ADP-ribose
-
-
?
ADP-glucose + H2O
AMP + alpha-D-glucose 1-phosphate
about 70% of the activity with ADP-mannose
-
-
?
ADP-mannose + H2O
AMP + D-mannose 1-phosphate
-
at 70% of the activity with ADPribose
-
-
?
ADP-mannose + H2O
AMP + D-mannose 1-phosphate
103% of the activity with ADP-ribose
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
the enzyme may have a predominant role in free ADP-ribose turnover and as a protective agent preventing the accumulation of this potential dangerous metabolite
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
protective enzyme whose function is to limit the intracellular accumulation of ADP-ribose
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
the enzyme plays important roles in controlling the intracellular levels of ADPR and preventing non-enzymatic ADP-ribosylation of proteins by hydrolyzing ADPR to AMP and ribose 5?-phosphate
-
-
?
ADP-ribose + H2O
AMP + ribose 5-phosphate
the function of the enzyme might be to remove free ADP-ribose arising from NAD+ and protein-bound poly- and non-enzymic protein glycation
-
-
?
ADP-ribose + H2O
AMP + ribose 5-phosphate
about 65% of the activity with ADP-mannose
-
-
?
ADP-ribose + H2O
AMP + ribose 5-phosphate
ADP-ribose is a better substrate compared with 8-oxo-dGDP
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
-
the enzyme may play an important role in the regulation of intracellular steady-state of free ADPribose
-
-
?
GDP-glucose + H2O
GMP + glucose 5-phosphate
7% of the activity with ADP-ribose
-
-
?
GDP-glucose + H2O
GMP + glucose 5-phosphate
about 15% of the activity with ADP-mannose
-
-
?
GDP-mannose + H2O
GMP + D-mannose 1-phosphate
-
at 40% of the activity with ADPribose
-
-
?
GDP-mannose + H2O
GMP + D-mannose 1-phosphate
about 15% of the activity with ADP-mannose
-
-
?
IDP-ribose + H2O
IMP + ribose 5-phosphate
-
at 59% of the activity with ADPribose
-
-
?
IDP-ribose + H2O
IMP + ribose 5-phosphate
9% of the activity with ADP-ribose
-
-
?
UDP-glucose + H2O
UMP + glucose 5-phosphate
-
at 5% of the activity with ADPribose
-
-
?
UDP-glucose + H2O
UMP + glucose 5-phosphate
about 12% of the activity with ADP-mannose
-
-
?
UDP-mannose + H2O
UMP + D-mannose 1-phosphate
-
at 20% of the activity with ADPribose
-
-
?
UDP-mannose + H2O
UMP + D-mannose 1-phosphate
about 15% of the activity with ADP-mannose
-
-
?
additional information
?
-
-
no activity with ADPglucose, ADPmannose, UDPglucose
-
-
?
additional information
?
-
-
hNUDT5 can utilize a variety of ADP-sugar conjugates as substrate, with a preference for ADPR
-
-
?
additional information
?
-
hNUDT5 can utilize a variety of ADP-sugar conjugates as substrate, with a preference for ADPR
-
-
?
additional information
?
-
ADP-ribose/CDP-alcohol diphosphatase (ADPRibase-Mn) acts as cyclic ADP-ribose (cADPR) phosphohydrolase with much lower efficiency than on its major substrates
-
-
-
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-ribose + H2O
AMP + ribose 5-phosphate
the function of the enzyme might be to remove free ADP-ribose arising from NAD+ and protein-bound poly- and non-enzymic protein glycation
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
-
the enzyme may play an important role in the regulation of intracellular steady-state of free ADPribose
-
-
?
additional information
?
-
ADP-ribose/CDP-alcohol diphosphatase (ADPRibase-Mn) acts as cyclic ADP-ribose (cADPR) phosphohydrolase with much lower efficiency than on its major substrates
-
-
-
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
the enzyme may have a predominant role in free ADP-ribose turnover and as a protective agent preventing the accumulation of this potential dangerous metabolite
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
protective enzyme whose function is to limit the intracellular accumulation of ADP-ribose
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
the enzyme plays important roles in controlling the intracellular levels of ADPR and preventing non-enzymatic ADP-ribosylation of proteins by hydrolyzing ADPR to AMP and ribose 5?-phosphate
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Zn2+
Mg2+
-
strictly requires Mg2+ (more than 1 mM) or Mn2+ for full activity. Treatment with H2O2 changes the specificity of both ADP-ribose activities for the activating divalent cation, giving them a marked preference for Mn2+ and rendering them virtually inactive with Mg2+
Mn2+
-
maximal activity at 0.02-0.05 mM with a steep decrease at increasing pH-values, Mg2+ or Mn2+ required
Mn2+
-
strictly requires Mg2+ or Mn2+ (0.05 mM) for full activity. Treatment with H2O2 changes the specificity of both ADP-ribose activities for the activating divalent cation, giving them a marked preference for Mn2+ and rendering them virtually inactive with Mg2+
Mn2+
the ADP-ribose pyrophosphatase reaction in crystalline state is conducted by consecutive binding of two Mn(II) ions as cofactors
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8-oxo-dGDP
the ADP-ribose cleavage is competitively inhibited by 8-oxo-dGDP (68% relative cleavage efficiency at 0.01 mM)
8-oxo-dGMP
the ADP-ribose cleavage is competitively inhibited by 8-oxo-dGMP (89% relative cleavage efficiency at 0.01 mM)
ADP-ribose
the 8-oxo-dGDP cleavage is competitively inhibited by ADP-ribose (22% relative cleavage efficiency at 0.005 mM)
fluoride
-
inhibition of Mg2+-dependent activity of ADP-ribose pyrophosphatase. the Mn2+-dependent activity is not affected by fluoride
AMP
the 8-oxo-dGDP cleavage is competitively inhibited by AMP (30% relative cleavage efficiency at 0.005 mM)
N-acetyl-p-benzoquinoneimine
1 mM, almost complete inhibition of activity towards ADPribose. The inhibitor is a useful tool for distinguishing the specific ADP-ribose diphosphatase from the less specific ADP-sugar diphosphatases
additional information
no inhibitory effect is observed with 8-oxo-dGMP
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
nitric oxide
-
NO stimulates non-enzymatic ADP-ribosylation, at cysteine residues in the presence of reductant, of NUDT5 using ADP-ribose and consequently activates its ADPRase activity. ADPRase activity in J774 macrophage cells is increased by the treatment with SNP, an exogenous NO generator, or TNF-alpha/IFN-gamma, endogenous NO inducers. NO has a regulatory role, overview
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic analysis, Trp28 and Trp46 function synergistically in substrate binding and catalysis, overview
-
additional information
additional information
kinetic analysis, Trp28 and Trp46 function synergistically in substrate binding and catalysis, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9
activity at pH 8.0 is about 90% of the activity at pH 6.5 and at pH 9.0, activity with ADP-ribose
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 10
pH 4.5: about 55% of maximal activity, pH 10.0: about 50% of maximal activity, activity with ADP-mannose
6 - 10
pH 6.0: about 25% of maximal activity, pH 10.0: about 60% of maximal activity, activity with ADP-ribose
7 - 9
-
linearly decreasing activity profile from pH 7 to pH 9, with activity at pH 9 being 50% of that at pH 7
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
ADPRibase-Mn enzymes contain the dinuclear metal centre typical of the metallo-dependent phosphatases SCOP2 superfamily, forming within it a family of their own named as ADPRibase-Mn-like. ADPRibase-Mn proteins constitute also a functional family in the CATH classification, within cluster SC:3 of superfamily 3.60.21.10
physiological function
cyclic ADP-ribose (cADPR) is a messenger for Ca2+ mobilization. Its turnover is believed to occur by glycohydrolysis to ADP-ribose. ADP-ribose/CDP-alcohol diphosphatase (ADPRibase-Mn) acts as cADPR phosphohydrolase with much lower efficiency than on its major substrates
additional information
the ADP-ribose pyrophosphatase reaction in crystalline state is conducted by consecutive binding of two Mn(II) ions as cofactors. Amino acid sequence (with Nudix motif and substrate binding site)and structure comparisons of cytosolic ADPRases from Thermus thermophilus HB8 (Ndx4 and Ndx2), Mycobacterium tuberculosis (MtADPRase), Escherichia coli (EcADPRase), and humans (NUDT5), overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NUDT9_HUMAN
350
0
39125
Swiss-Prot
Mitochondrion (Reliability: 5)
ADPRM_HUMAN
342
0
39529
Swiss-Prot
other Location (Reliability: 1)
NUDT5_HUMAN
219
0
24328
Swiss-Prot
other Location (Reliability: 1)
W0NWJ0_HUMAN
342
0
39529
TrEMBL
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
85000
dimeric thioredoxin fusion protein expressed in Escherichia coli, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complexed with 8-oxo-dGMP, 8-oxo-dGDP and 8-oxo-dADP, hanging drop vapor diffusion method, using 0.8 M NaH2PO4/1.2M K2HPO4 and 0.1 M acetate (pH 4.5), and 0.2M ammonium acetate, 35-40% (w/v) polyethylene glycol 3350 and 0.1 M sodium citrate (pH 6.2)
in apo form, in complex with ADP-D-ribose, and in complex with AMP with bound Mg2+, hanging drop vapor diffusion method, using 160 mM sodium acetate (pH 5.5), and 25% (w/v) 2-methyl-2,4-pentanediol, or 300 mM di-ammonium hydrogen citrate, 6% (w/v) n-propanol and 15% (w/v) polyethylene glycol 3350, or 200 mM sodium acetate, 100 mM Tris-HCl (pH 8.0) and 30% (w/v) polyethylene glycol 4000
in complex with alpha,beta-methyleneadenosine diphosphoribose and 3 Mg2+ ions, hanging drop vapor diffusion method, using 250 mM sodium acetate, 100 mM Tris-HCl, pH 8.0, and 29% (w/v) polyethylene glycol 4000
purified recombinant wild-type and truncated mutant NUDT5 in complex with a non-hydrolyzable ADPR analogue, alpha,beta-methyleneadenosine diphosphoribose, and three Mg2+ ions representing the transition state of the enzyme during catalysis, 20 mg/ml protein is incubated with 5 mM AMPCPR and 10 mM MgCl2 at 4 °C overnight, followed by hanging drop vapour diffusion method, wild-type enzyme in complex with AMPCPR, and truncation mutant DELTAhNUDT5 in complex with AMPCPR and Mg2+, 4 °C, mixing of equal volumes of the protein solution and the reservoir solution containing 250 mM NaAc, 100 mM Tris-HCl, pH 8.0, and 29% PEG 4000, ingle crystals of the plate-shape morphology grow after 1 month, X-ray diffraction structure determination and anaylsis at 2.0 A resolution, molecular modelling
substrate docking on a homology model suggests possible interactions of ADP-ribose with seven residues located, with one exception (Cys253), either within the metallo-dependent phosphatases signature (Gln27, Asn110, His111), or in unique structural regions of the ADPRibase-Mn family: s2s3 (Phe37 and Arg43) and h7h8 (Phe210), around the active site entrance. Residue Phe37 is needed for ADP-ribose preference without catalytic effect. Arg43 is essential for catalysis. Cys253 is hindering for cADPR phosphohydrolase
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-Sepharose 6 column chromatography, HisTrap column chromatography, and Superdex 75 gel filtration
recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 by glutathione affinity chromatography, proteolytic tag cleavage
recombinant His6-tagged NUDT5 from Escherichia coli strain BL21 by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
gene ADPRM, cloned from liver, recombinant expression of GST-tagged wild-type and mutant enzymes in Escherichia coli strain BL21
gene NUDT5, expression in murine J774A.1 macrophage cells, expression of His6-tagged NUDT5 in Escherichia coli strain BL21
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kim, Y.P.; Kahng, J.B.; Choi, J.Y.
Adenosine diphosphate ribose pyrophosphohydrolase in human skin
J. Dermatol.
7
11-15
1980
Homo sapiens
Kim, J.S.; Kim, W.Y.; Rho, H.W.; Park, J.W.; Park, B.H.; Han, M.K.; Kim, U.H.; Kim, H.R.
Purification and characterization of adenosine diphosphate ribose pyrophosphatase from human erythrocytes
Int. J. Biochem. Cell Biol.
30
629-638
1998
Homo sapiens
Gasmi, L.; Cartwright, J.L.; McLennan, A.G.
Cloning, expression and characterization of YSA1H, a human adenosine 5'-diphosphosugar pyrophosphatase possessing a MutT motif
Biochem. J.
344
331-337
1999
Homo sapiens (Q9UKK9), Homo sapiens
Ribeiro, J.M.; Carloto, A.; Costas, M.J.; Cameselle, J.C.
Human placenta hydrolases active on free ADP-ribose: an ADP-sugar pyrophosphatase and a specific ADP-ribose pyrophosphatase
Biochim. Biophys. Acta
1526
86-94
2001
Homo sapiens
Lin, S.; Gasmi, L.; Xie, Y.; Ying, K.; Gu, S.; Wang, Z.; Jin, H.; Chao, Y.; Wu, C.; Zhou, Z.; Tang, R.; Mao, Y.; McLennan, A.G.
Cloning, expression and characterisation of a human Nudix hydrolase specific for adenosine 5'-diphosphoribose (ADP-ribose)
Biochim. Biophys. Acta
1594
127-135
2001
Homo sapiens (Q9BW91), Homo sapiens
Yang, H.; Slupska, M.M.; Wei, Y.F.; Tai, J.H.; Luther, W.M.; Xia, Y.R.; Shih, D.M.; Chiang, J.H.; Baikkalov, C.; Fitz-Gibbon, S.; Phan, I.T.; Conrad, A.; Miller, J.H.
Cloning and characterization of a new member of nudix hydrolases from human and mouse
J. Biol. Chem.
275
8844-8853
2000
Homo sapiens (Q9UKK9), Homo sapiens, Mus musculus
Perraud, A.L.; Shen, B.; Dunn, C.A.; Rippe, K.; Smith, M.K.; Bessman, M.J.; Stoddard, B.L.; Scharenberg, A.M.
NUDT9, a member of the Nudix hydrolase family, is an evolutionarily conserved mitochondrial ADP-ribose pyrophosphatase
J. Biol. Chem.
278
1794-1801
2003
Homo sapiens
Carloto, A.; Costas, M.J.; Cameselle, J.C.; McLennan, A.G.; Ribeiro, J.M.
The specific, submicromolar-K(m) ADP-ribose pyrophosphatase purified from human placenta is enzymically indistinguishable from recombinant NUDT9 protein, including a selectivity for Mn(2+) as activating cation and increase in K(m) for ADP-ribose, both eli
Biochim. Biophys. Acta
1760
1545-1551
2006
Homo sapiens
Yu, H.N.; Song, E.K.; Yoo, S.M.; Lee, Y.R.; Han, M.K.; Yim, C.Y.; Kwak, J.Y.; Kim, J.S.
Activation of NUDT5, an ADP-ribose pyrophosphatase, by nitric oxide-mediated ADP-ribosylation
Biochem. Biophys. Res. Commun.
354
764-768
2007
Homo sapiens
Zha, M.; Guo, Q.; Zhang, Y.; Yu, B.; Ou, Y.; Zhong, C.; Ding, J.
Molecular mechanism of ADP-ribose hydrolysis by human NUDT5 from structural and kinetic studies
J. Mol. Biol.
379
568-578
2008
Homo sapiens, Homo sapiens (Q9UKK9)
Ito, R.; Sekiguchi, M.; Setoyama, D.; Nakatsu, Y.; Yamagata, Y.; Hayakawa, H.
Cleavage of oxidized guanine nucleotide and ADP sugar by human NUDT5 protein
J. Biochem.
149
731-738
2011
Homo sapiens (Q9UKK9), Homo sapiens
Zha, M.; Zhong, C.; Peng, Y.; Hu, H.; Ding, J.
Crystal structures of human NUDT5 reveal insights into the structural basis of the substrate specificity
J. Mol. Biol.
364
1021-1033
2006
Homo sapiens (Q9UKK9), Homo sapiens
Cabezas, A.; Ribeiro, J.; Rodrigues, J.; Lopez-Villamizar, I.; Fernandez, A.; Canales, J.; Pinto, R.; Costas, M.; Cameselle, J.
Molecular bases of catalysis and ADP-ribose preference of human Mn2+-dependent adpribose/CDP-alcohol diphosphatase and conversion by mutagenesis to a preferential cyclic ADP-ribose phosphohydrolase
PLoS ONE
10
e0118680
2015
Homo sapiens (W0NWJ0), Homo sapiens
Arimori, T.; Tamaoki, H.; Nakamura, T.; Kamiya, H.; Ikemizu, S.; Takagi, Y.; Ishibashi, T.; Harashima, H.; Sekiguchi, M.; Yamagata, Y.
Diverse substrate recognition and hydrolysis mechanisms of human NUDT5
Nucleic Acids Res.
39
8972-8983
2011
Homo sapiens (Q9UKK9), Homo sapiens
Furuike, Y.; Akita, Y.; Miyahara, I.; Kamiya, N.
ADP-ribose pyrophosphatase reaction in crystalline state conducted by consecutive binding of two manganese (II) ions as cofactors
Biochemistry
55
1801-1812
2016
Escherichia coli (Q93K97), Homo sapiens (Q9UKK9), Mycobacterium tuberculosis (O33199), Mycobacterium tuberculosis CDC 1551 (O33199), Mycobacterium tuberculosis Oshkosh (O33199), Thermus thermophilus, Thermus thermophilus (Q84CU3)
Ribeiro, J.M.; Canales, J.; Cabezas, A.; Rodrigues, J.R.; Pinto, R.M.; Lopez-Villamizar, I.; Costas, M.J.; Cameselle, J.C.
Specific cyclic ADP-ribose phosphohydrolase obtained by mutagenic engineering of Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase
Sci. Rep.
8
1036
2018
Homo sapiens (Q3LIE5)
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