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Information on EC 3.6.1.13 - ADP-ribose diphosphatase and Organism(s) Escherichia coli and UniProt Accession Q93K97

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EC Tree
     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.13 ADP-ribose diphosphatase
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This record set is specific for:
Escherichia coli
UNIPROT: Q93K97 not found.
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ADP-ribose pyrophosphatase
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adenosine diphosphoribose pyrophosphatase
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-
-
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ADP-ribose diphosphatase
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-
-
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ADP-ribose phosphohydrolase
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-
-
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ADP-ribose pyrophosphatase
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-
-
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ADPR-PPase
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-
-
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ADPRibase
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-
-
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ADPribose pyrophosphatase
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-
-
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pyrophosphatase, adenosine diphosphoribose
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphorous acid anhydride hydrolysis
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-
-
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
ADP-D-ribose ribophosphohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9024-83-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADPribose + H2O
AMP + D-ribose 5-phosphate
show the reaction diagram
ADPribose + H2O
AMP + D-ribose 5-phosphate
show the reaction diagram
GDP-mannose + H2O
GMP + D-mannose 1-phosphate
show the reaction diagram
-
-
-
-
?
NADH + H2O
?
show the reaction diagram
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at 9% of the activity with ADPribose
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADPribose + H2O
AMP + D-ribose 5-phosphate
show the reaction diagram
-
the enzyme may play a role in tellurite resistance
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
dependent on
Mn2+
the ADP-ribose pyrophosphatase reaction in crystalline state is conducted by consecutive binding of two Mn(II) ions as cofactors
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.067
ADPribose
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
117
ADPribose
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-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion at 18°C. The structure of the apo enzyme, the active enzyme and the complex with ADP-ribose are determined to 1.9 A, 2.7 A and 2.3 A, respectively. The Nudix motif residues, folded as a loop-helix-loop tailored for diphosphate hydrolysis, compose the catalytic center
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dunn, C.A.; OHandley, S.F.; Frick, D.N.; Bessman, M.J.
Studies on the ADP-ribose pyrophosphatase subfamily of the nudix hydrolases and tentative identification of trgB, a gene associated with tellurite resistance
J. Biol. Chem.
274
32318-32324
1999
Bacillus subtilis (P54570), Bacillus subtilis, Cereibacter sphaeroides, Escherichia coli, Haemophilus influenzae (P44684), Methanocaldococcus jannaschii, Saccharomyces cerevisiae
Manually annotated by BRENDA team
Gabelli, S.B.; Bianchet, M.A.; Ohnishi, Y.; Ichikawa, Y.; Bessman, M.J.; Amzel, L.M.
Mechanism of the Escherichia coli ADP-ribose pyrophosphatase, a Nudix hydrolase
Biochemistry
41
9279-9285
2002
Escherichia coli (Q93K97), Escherichia coli
Manually annotated by BRENDA team
Gabelli, S.B.; Bianchet, M.A.; Bessman, M.J.; Amzel, L.M.
The structure of ADP-ribose pyrophosphatase reveals the structural basis for the versatility of the Nudix family
Nat. Struct. Biol.
8
467-472
2001
Escherichia coli (Q93K97), Escherichia coli
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team