BRENDA - Enzyme Database
show all sequences of 3.6.1.61

The Nudix hydrolase Ndx1 from Thermus thermophilus HB8 is a diadenosine hexaphosphate hydrolase with a novel activity

Iwai, T.; Kuramitsu, S.; Masui, R.; J. Biol. Chem. 279, 21732-21739 (2004)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
overexpressed in Escherichia coli
Thermus thermophilus
Engineering
Amino acid exchange
Commentary
Organism
E46Q
2200fold reduction in kcat
Thermus thermophilus
E49Q
mutation has very little effect on activity
Thermus thermophilus
E50Q
130000fold reduction in kcat
Thermus thermophilus
W26S
no decrease in fluorescence intensity upon the addition of ATP
Thermus thermophilus
Inhibitors
Inhibitors
Commentary
Organism
Structure
ATP
-
Thermus thermophilus
dATP
-
Thermus thermophilus
fluoride
non-competitive inhibition
Thermus thermophilus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0014
-
P1,P6-bis(5'-adenosyl)hexaphosphate
pH 7.0, 25°C
Thermus thermophilus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
Ndx1 activity requires the presence of the divalent cations Mn2+, Mg2+, Zn2+, and Co2+
Thermus thermophilus
Mg2+
Ndx1 activity requires the presence of the divalent cations Mn2+, Mg2+, Zn2+, and Co2+
Thermus thermophilus
Mn2+
Ndx1 activity requires the presence of the divalent cations Mn2+, Mg2+, Zn2+, and Co2+
Thermus thermophilus
additional information
Ca2+, Ni2+, and Cu2+ are not able to activate Ndx1
Thermus thermophilus
Zn2+
Ndx1 activity requires the presence of the divalent cations Mn2+, Mg2+, Zn2+, and Co2+
Thermus thermophilus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
14170
-
1 * 14170, calculated from sequence
Thermus thermophilus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
Thermus thermophilus
-
2 ATP
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Thermus thermophilus
Q75UV1
-
-
Purification (Commentary)
Commentary
Organism
-
Thermus thermophilus
Reaction
Reaction
Commentary
Organism
P1,P4-bis(5'-adenosyl)tetraphosphate + H2O = ATP + AMP
nucleophilic double, not single, displacement catalytic forward reaction mechanism via oxocarbenium ion intermediate, detailed overview
Thermus thermophilus
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O = ATP + ADP
(2)
Thermus thermophilus
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O = 2 ATP
(1)
Thermus thermophilus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
P1,P4-bis(5'-adenosyl)tetraphosphate + H2O
-
715466
Thermus thermophilus
ATP + AMP
-
-
-
?
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
-
715466
Thermus thermophilus
ATP + ADP
-
-
-
?
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
-
715466
Thermus thermophilus
2 ATP
-
-
-
?
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
P1,P6-bis(5'-adenosyl)hexaphosphate is the most preferred substrate. Glu46 and Glu50 are conserved residues in the Nudix motif and are involved in catalysis
715466
Thermus thermophilus
2 ATP
-
-
-
?
Subunits
Subunits
Commentary
Organism
monomer
1 * 14170, calculated from sequence
Thermus thermophilus
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
70
-
hydrolysis of P1,P6-bis(5'-adenosyl)hexaphosphate
Thermus thermophilus
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
95
-
pH 7.5, stable up to
Thermus thermophilus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4.1
-
P1,P6-bis(5'-adenosyl)hexaphosphate
pH 7.0, 25°C
Thermus thermophilus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
hydrolysis of P1,P6-bis(5'-adenosyl)hexaphosphate
Thermus thermophilus
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
2
12
25°C, stable
Thermus thermophilus
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.013
-
ATP
pH 7.0, 25°C
Thermus thermophilus
0.041
-
dATP
pH 7.0, 25°C
Thermus thermophilus
0.424
-
fluoride
pH 7.0, 25°C
Thermus thermophilus
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Thermus thermophilus
calculated from sequence
-
4.8
IC50 Value
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.08
-
pH 7.0, 25°C
Thermus thermophilus
fluoride
Cloned(Commentary) (protein specific)
Commentary
Organism
overexpressed in Escherichia coli
Thermus thermophilus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
E46Q
2200fold reduction in kcat
Thermus thermophilus
E49Q
mutation has very little effect on activity
Thermus thermophilus
E50Q
130000fold reduction in kcat
Thermus thermophilus
W26S
no decrease in fluorescence intensity upon the addition of ATP
Thermus thermophilus
IC50 Value (protein specific)
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.08
-
pH 7.0, 25°C
Thermus thermophilus
fluoride
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
ATP
-
Thermus thermophilus
dATP
-
Thermus thermophilus
fluoride
non-competitive inhibition
Thermus thermophilus
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.013
-
ATP
pH 7.0, 25°C
Thermus thermophilus
0.041
-
dATP
pH 7.0, 25°C
Thermus thermophilus
0.424
-
fluoride
pH 7.0, 25°C
Thermus thermophilus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0014
-
P1,P6-bis(5'-adenosyl)hexaphosphate
pH 7.0, 25°C
Thermus thermophilus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
Ndx1 activity requires the presence of the divalent cations Mn2+, Mg2+, Zn2+, and Co2+
Thermus thermophilus
Mg2+
Ndx1 activity requires the presence of the divalent cations Mn2+, Mg2+, Zn2+, and Co2+
Thermus thermophilus
Mn2+
Ndx1 activity requires the presence of the divalent cations Mn2+, Mg2+, Zn2+, and Co2+
Thermus thermophilus
additional information
Ca2+, Ni2+, and Cu2+ are not able to activate Ndx1
Thermus thermophilus
Zn2+
Ndx1 activity requires the presence of the divalent cations Mn2+, Mg2+, Zn2+, and Co2+
Thermus thermophilus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
14170
-
1 * 14170, calculated from sequence
Thermus thermophilus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
Thermus thermophilus
-
2 ATP
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Thermus thermophilus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
P1,P4-bis(5'-adenosyl)tetraphosphate + H2O
-
715466
Thermus thermophilus
ATP + AMP
-
-
-
?
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
-
715466
Thermus thermophilus
ATP + ADP
-
-
-
?
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
-
715466
Thermus thermophilus
2 ATP
-
-
-
?
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
P1,P6-bis(5'-adenosyl)hexaphosphate is the most preferred substrate. Glu46 and Glu50 are conserved residues in the Nudix motif and are involved in catalysis
715466
Thermus thermophilus
2 ATP
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 14170, calculated from sequence
Thermus thermophilus
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
70
-
hydrolysis of P1,P6-bis(5'-adenosyl)hexaphosphate
Thermus thermophilus
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
95
-
pH 7.5, stable up to
Thermus thermophilus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4.1
-
P1,P6-bis(5'-adenosyl)hexaphosphate
pH 7.0, 25°C
Thermus thermophilus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
hydrolysis of P1,P6-bis(5'-adenosyl)hexaphosphate
Thermus thermophilus
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
2
12
25°C, stable
Thermus thermophilus
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Thermus thermophilus
calculated from sequence
-
4.8
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
2929
-
P1,P6-bis(5'-adenosyl)hexaphosphate
pH 7.0, 25°C
Thermus thermophilus
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
2929
-
P1,P6-bis(5'-adenosyl)hexaphosphate
pH 7.0, 25°C
Thermus thermophilus
Other publictions for EC 3.6.1.61
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)
714017
Zheng
Homology modeling and substrat ...
Thermus thermophilus
Biochem. Biophys. Res. Commun.
333
881-887
2005
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-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
715466
Iwai
The Nudix hydrolase Ndx1 from ...
Thermus thermophilus
J. Biol. Chem.
279
21732-21739
2004
-
-
1
-
4
-
3
1
-
5
1
1
-
1
-
-
1
3
-
-
-
-
4
1
1
-
1
1
1
-
1
-
3
1
1
-
-
1
-
-
4
-
1
3
3
1
-
5
1
1
-
-
-
1
-
-
-
-
4
1
1
-
1
1
1
-
1
1
-
-
-
-
1
1
715453
Bessman
The gene ygdP, associated with ...
Escherichia coli
J. Biol. Chem.
276
37834-37838
2001
-
-
1
-
-
-
-
2
-
3
1
-
-
1
-
-
1
-
-
-
-
-
4
-
1
-
-
2
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
2
-
3
1
-
-
-
-
1
-
-
-
-
4
-
1
-
-
2
2
-
-
-
-
-
-
-
2
2