BRENDA - Enzyme Database
show all sequences of 3.1.11.7

Aprataxin forms a discrete branch in the HIT (histidine triad) superfamily of proteins with both DNA/RNA binding and nucleotide hydrolase activities

Kijas, A.W.; Harris, J.L.; Harris, J.M.; Lavin, M.F.; J. Biol. Chem. 281, 13939-13948 (2006)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Saccharomyces cerevisiae
Homo sapiens
Engineering
Amino acid exchange
Commentary
Organism
additional information
removal of the N-terminal forkhead associated domain does not alter activity with substrates AMPNH2 and Ap4A
Homo sapiens
V263G
mutation identified in a AOA1 patient, mutant protein is unable to bind DNA
Homo sapiens
Inhibitors
Inhibitors
Commentary
Organism
Structure
Duplex DNA
significantly reduces catalytic catalytic activity on the model histidine triad nucleotide-binding protein substrate, AMPNH2, and the Fragile histidine triad protein substrate, Ap4A
Homo sapiens
single-strand DNA
reduces catalytic catalytic activity on the model histidine triad nucleotide-binding protein substrate, AMPNH2, and the Fragile histidine triad protein substrate, Ap4A
Homo sapiens
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.018
-
P1,P4-bis(5'-adenosyl)tetraphosphate
pH 7.0, 30°C
Homo sapiens
0.837
-
adenosine-5'-monophosphoramidate
pH 7.0, 30°C
Homo sapiens
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
Q7Z2E3
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
adenosine-5'-monophosphoramidate + H2O
-
740679
Homo sapiens
AMP + NH3
-
-
-
?
ATP + H2O
-
740679
Homo sapiens
AMP + diphosphate
-
-
-
?
additional information
aprataxin hydrolyzes with similar efficiency the model histidine triad nucleotide-binding protein substrate : adenosine-5'-monophosphoramidate, AMPNH2, and the Fragile histidine triad protein substrate, Ap4A. No substrate: dATP
740679
Homo sapiens
?
-
-
-
-
P1,P4-bis(5'-adenosyl)tetraphosphate + H2O
-
740679
Homo sapiens
AMP + ATP
-
-
-
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0115
-
P1,P4-bis(5'-adenosyl)tetraphosphate
pH 7.0, 30°C
Homo sapiens
0.0195
-
adenosine-5'-monophosphoramidate
pH 7.0, 30°C
Homo sapiens
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Saccharomyces cerevisiae
Homo sapiens
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
removal of the N-terminal forkhead associated domain does not alter activity with substrates AMPNH2 and Ap4A
Homo sapiens
V263G
mutation identified in a AOA1 patient, mutant protein is unable to bind DNA
Homo sapiens
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Duplex DNA
significantly reduces catalytic catalytic activity on the model histidine triad nucleotide-binding protein substrate, AMPNH2, and the Fragile histidine triad protein substrate, Ap4A
Homo sapiens
single-strand DNA
reduces catalytic catalytic activity on the model histidine triad nucleotide-binding protein substrate, AMPNH2, and the Fragile histidine triad protein substrate, Ap4A
Homo sapiens
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.018
-
P1,P4-bis(5'-adenosyl)tetraphosphate
pH 7.0, 30°C
Homo sapiens
0.837
-
adenosine-5'-monophosphoramidate
pH 7.0, 30°C
Homo sapiens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
adenosine-5'-monophosphoramidate + H2O
-
740679
Homo sapiens
AMP + NH3
-
-
-
?
ATP + H2O
-
740679
Homo sapiens
AMP + diphosphate
-
-
-
?
additional information
aprataxin hydrolyzes with similar efficiency the model histidine triad nucleotide-binding protein substrate : adenosine-5'-monophosphoramidate, AMPNH2, and the Fragile histidine triad protein substrate, Ap4A. No substrate: dATP
740679
Homo sapiens
?
-
-
-
-
P1,P4-bis(5'-adenosyl)tetraphosphate + H2O
-
740679
Homo sapiens
AMP + ATP
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0115
-
P1,P4-bis(5'-adenosyl)tetraphosphate
pH 7.0, 30°C
Homo sapiens
0.0195
-
adenosine-5'-monophosphoramidate
pH 7.0, 30°C
Homo sapiens
General Information
General Information
Commentary
Organism
physiological function
aprataxin has dual DNA binding and nucleotide hydrolase activities. The protein binds to double-stranded DNA with high affinity but is also capable of binding double-stranded RNA and single-strand DNA, with increased affinity for hairpin structures. The DNA binding is not dependent on zinc
Homo sapiens
General Information (protein specific)
General Information
Commentary
Organism
physiological function
aprataxin has dual DNA binding and nucleotide hydrolase activities. The protein binds to double-stranded DNA with high affinity but is also capable of binding double-stranded RNA and single-strand DNA, with increased affinity for hairpin structures. The DNA binding is not dependent on zinc
Homo sapiens
Other publictions for EC 3.1.11.7
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
750390
Horton
XRCC1 phosphorylation affects ...
Homo sapiens, Saccharomyces cerevisiae
DNA Repair
64
26-33
2018
-
-
2
-
1
-
-
-
1
-
-
2
-
2
-
-
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1
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4
-
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2
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2
2
-
1
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1
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2
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-
-
1
-
-
4
-
-
-
-
-
-
-
-
-
-
4
4
-
-
-
750417
Tumbale
Mechanism of APTX nicked DNA ...
Homo sapiens
EMBO J.
37
e98875
2018
-
-
1
1
26
-
-
2
-
1
-
1
-
2
-
-
1
-
-
-
-
-
3
-
1
-
-
2
1
-
-
-
-
-
-
-
-
1
-
1
26
-
-
-
-
2
-
1
-
1
-
-
-
1
-
-
-
-
3
-
1
-
-
2
1
-
-
-
-
2
2
-
2
2
741077
Chauleau
DNA3pp5G de-capping activity o ...
Schizosaccharomyces pombe, Schizosaccharomyces pombe ATCC 24843
Nucleic Acids Res.
43
6075-6083
2015
-
-
-
1
-
-
-
-
-
-
-
-
-
5
-
-
-
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-
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2
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1
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-
2
-
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-
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-
-
-
-
-
-
-
-
-
-
750307
Hanaoka
-
A QM/MM study of the 5'-AMP D ...
Homo sapiens
Chem. Phys. Lett.
631-632
16-20
2015
-
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
2
-
-
-
-
1
-
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1
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1
-
-
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-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
4
4
-
-
-
750720
Garcia-Diaz
Lack of aprataxin impairs mit ...
Homo sapiens
Hum. Mol. Genet.
24
4516-4529
2015
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
4
-
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2
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-
-
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-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
752086
Schellenberg
Molecular underpinnings of Ap ...
Homo sapiens
Prog. Biophys. Mol. Biol.
117
157-165
2015
-
-
-
-
15
-
-
-
-
1
-
1
-
2
-
-
-
2
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
15
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
3
3
-
-
-
741062
Tumbale
Aprataxin resolves adenylated ...
Homo sapiens, Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508
Nature
506
111-115
2014
-
-
-
1
1
-
-
4
-
-
-
4
-
5
-
-
-
-
-
-
-
-
6
-
-
-
-
4
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-
1
1
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4
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4
-
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-
-
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-
-
-
6
-
-
-
-
4
-
-
-
-
-
2
2
-
4
4
741058
Tumbale
Structure of an aprataxin-DNA ...
Schizosaccharomyces pombe, Schizosaccharomyces pombe ATCC 24843
Nat. Struct. Mol. Biol.
18
1189-1195
2011
-
-
-
1
3
-
-
-
-
-
-
-
-
6
-
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-
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-
4
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1
3
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-
4
-
-
-
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-
-
-
-
-
-
-
-
-
741059
Gong
Crystal structures of aprataxi ...
Schizosaccharomyces pombe, Schizosaccharomyces pombe ATCC 24843
Nat. Struct. Mol. Biol.
18
1297-1299
2011
-
-
-
1
-
-
-
-
-
-
-
-
-
6
-
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1
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-
740352
Daley
Genetic interactions between H ...
Saccharomyces cerevisiae
DNA Repair
9
690-699
2010
-
-
-
-
-
-
-
-
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2
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1
1
-
-
-
741072
Becherel
CK2 phosphorylation-dependent ...
Homo sapiens
Nucleic Acids Res.
38
1489-1503
2010
-
-
-
1
1
-
-
-
1
-
-
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-
1
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-
2
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1
1
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1
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2
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-
1
1
-
-
-
703960
Harris
Aprataxin, poly-ADP ribose pol ...
Homo sapiens
Hum. Mol. Genet.
18
4102-4117
2009
-
1
-
-
-
-
-
-
-
-
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1
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1
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-
1
1
-
-
-
740519
Becherel
Nucleolar localization of apra ...
Homo sapiens
Hum. Mol. Genet.
15
2239-2249
2006
-
1
-
-
-
-
-
-
1
-
-
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-
2
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1
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1
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-
-
-
-
-
-
-
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-
1
1
-
-
-
740679
Kijas
Aprataxin forms a discrete bra ...
Homo sapiens
J. Biol. Chem.
281
13939-13948
2006
-
-
1
-
2
-
2
2
-
-
-
-
-
1
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4
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2
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1
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2
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2
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2
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4
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-
2
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1
1
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-
741060
Ahel
The neurodegenerative disease ...
Gallus gallus, Mus musculus
Nature
443
713-716
2006
-
-
-
-
-
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4
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2
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740277
Mosesso
The novel human gene aprataxin ...
Homo sapiens
Cell. Mol. Life Sci.
62
485-491
2005
-
1
-
-
1
-
-
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3
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1
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1
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-
-
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1
1
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-
-
740677
Seidle
Disease-associated mutations i ...
Homo sapiens
J. Biol. Chem.
280
20927-20931
2005
-
-
1
-
11
-
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2
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1
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3
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2
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1
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11
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2
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3
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2
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-
2
2
739862
Sano
Aprataxin, the causative prote ...
Homo sapiens
Ann. Neurol.
55
241-249
2004
-
-
-
-
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1
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2
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1
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1
1
1
1
-
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739976
Date
The FHA domain of aprataxin in ...
Homo sapiens
Biochem. Biophys. Res. Commun.
325
1279-1285
2004
-
-
-
-
-
-
-
-
-
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1
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1
1
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740518
Gueven
Aprataxin, a novel protein tha ...
Homo sapiens
Hum. Mol. Genet.
13
1081-1093
2004
-
1
-
-
-
-
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-
2
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2
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1
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1
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2
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1
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-
1
1
-
-
-
741055
Moreira
The gene mutated in ataxia-ocu ...
Homo sapiens
Nat. Genet.
29
189-193
2001
-
1
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-
-
-
1
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1
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