BRENDA - Enzyme Database
show all sequences of 3.6.1.17

Analysis of the catalytic and binding residues of the diadenosine tetraphosphate pyrophosphohydrolase from Caenorhabditis elegans by site-directed mutagenesis

Abdelghany, H.M.; Bailey, S.; Blackburn, G.M.; Rafferty, J.B.; McLennan, A.G.; J. Biol. Chem. 278, 4435-4439 (2003)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expression in Escherichia coli, mutant enzymes Y27A, Y27D, H31A, H31V, W32G, K36M, H38G, H38K, E52Q, E56Q, Y76A, Y76/Y121A, K79M, K81M, K83M, E103Q, Y121A
Caenorhabditis elegans
Engineering
Protein Variants
Commentary
Organism
E103Q
turnover-number for hydrolysis of Ap4A is 3.2% of that of the wild-type enzyme, KM-value is 66% of the wild-type value
Caenorhabditis elegans
E52Q
turnover-number for hydrolysis of Ap4A is 0.02% of that of the wild-type enzyme, KM-value is 60% of the wild-type value
Caenorhabditis elegans
E56Q
turnover-number for hydrolysis of Ap4A is 0.001% of that of the wild-type enzyme, KM-value is 90% of the wild-type value
Caenorhabditis elegans
H31A
turnover-number for hydrolysis of Ap4A is 52% of that of the wild-type enzyme, KM-value is 8.3fold higher than the KM-value of the wild-type enzyme
Caenorhabditis elegans
H31V
turnover-number for hydrolysis of Ap4A is 61% of that of the wild-type enzyme, KM-value is 12.5fold higher than the KM-value of the wild-type enzyme
Caenorhabditis elegans
H38G
turnover-number for hydrolysis of Ap4A is 135% of that of the wild-type enzyme, KM-value is 66% of the wild-type value
Caenorhabditis elegans
H38K
turnover-number for hydrolysis of Ap4A is 135% of that of the wild-type enzyme, KM-value is 47% of the wild-type value
Caenorhabditis elegans
K36M
turnover-number for hydrolysis of Ap4A is 9% of that of the wild-type enzyme, KM-value is 1.5fold higher than the KM-value of the wild-type enzyme
Caenorhabditis elegans
K79M
turnover-number for hydrolysis of Ap4A is 0.7% of that of the wild-type enzyme, KM-value is 1.7fold higher than the KM-value of the wild-type enzyme
Caenorhabditis elegans
K81M
turnover-number for hydrolysis of Ap4A is 130% of that of the wild-type enzyme, KM-value is 2.3fold higher than the KM-value of the wild-type enzyme
Caenorhabditis elegans
K83M
turnover-number for hydrolysis of Ap4A is 2.6% of that of the wild-type enzyme, KM-value is 15.9fold higher than the KM-value of the wild-type enzyme
Caenorhabditis elegans
Y121A
turnover-number for hydrolysis of Ap4A is 61% of that of the wild-type enzyme, KM-value is 8.5fold higher than the KM-value of the wild-type enzyme
Caenorhabditis elegans
Y27A
turnover-number for hydrolysis of Ap4A is 113% of that of the wild-type enzyme, KM-value is 1.25fold higher than the KM-value of the wild-type enzyme
Caenorhabditis elegans
Y27D
turnover-number for hydrolysis of Ap4A is 126% of that of the wild-type enzyme, KM-value is 1.8fold higher than the KM-value of the wild-type enzyme
Caenorhabditis elegans
Y76A
turnover-number for hydrolysis of Ap4A is 8.7% of that of the wild-type enzyme, KM-value is 6.7fold higher than the KM-value of the wild-type enzyme
Caenorhabditis elegans
Y76A/Y121A
turnover-number for hydrolysis of Ap4A is 4.8% of that of the wild-type enzyme, KM-value is 3.75fold higher than the KM-value of the wild-type enzyme
Caenorhabditis elegans
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0041
-
Ap4A
mutant enzyme H38K
Caenorhabditis elegans
0.0053
-
Ap4A
mutant enzyme E52Q
Caenorhabditis elegans
0.0058
-
Ap4A
mutant enzyme E103Q; mutant enzyme H38G
Caenorhabditis elegans
0.0079
-
Ap4A
mutant enzyme E56Q
Caenorhabditis elegans
0.0088
-
Ap4A
wild-type enzyme
Caenorhabditis elegans
0.011
-
Ap4A
mutant enzyme Y27A
Caenorhabditis elegans
0.013
-
Ap4A
mutant enzyme K36M
Caenorhabditis elegans
0.015
-
Ap4A
mutant enzyme K79M
Caenorhabditis elegans
0.016
-
Ap4A
mutant enzyme Y27D
Caenorhabditis elegans
0.02
-
Ap4A
mutant enzyme K81M
Caenorhabditis elegans
0.033
-
Ap4A
mutant enzyme Y76A/Y121A
Caenorhabditis elegans
0.059
-
Ap4A
mutant enzyme Y76A
Caenorhabditis elegans
0.073
-
Ap4A
mutant enzyme H31A
Caenorhabditis elegans
0.075
-
Ap4A
mutant enzyme Y121A
Caenorhabditis elegans
0.11
-
Ap4A
mutant enzyme H31V
Caenorhabditis elegans
0.14
-
Ap4A
mutant enzyme K83M
Caenorhabditis elegans
Organism
Organism
UniProt
Commentary
Textmining
Caenorhabditis elegans
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
diadenosine 5',5''-P1,P4-tetraphosphate + H2O
-
656173
Caenorhabditis elegans
ATP + AMP
-
-
-
?
Synonyms
Synonyms
Commentary
Organism
diadenosine tetraphosphate pyrophosphohydrolase
-
Caenorhabditis elegans
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.00024
-
Ap4A
mutant enzyme E56Q
Caenorhabditis elegans
0.0052
-
Ap4A
mutant enzyme E52Q
Caenorhabditis elegans
0.16
-
Ap4A
mutant enzyme K79M
Caenorhabditis elegans
0.6
-
Ap4A
mutant enzyme K83M
Caenorhabditis elegans
0.75
-
Ap4A
mutant enzyme E103Q
Caenorhabditis elegans
1.1
-
Ap4A
mutant enzyme Y76A/Y121A
Caenorhabditis elegans
2
-
Ap4A
mutant enzyme Y76A
Caenorhabditis elegans
2.1
-
Ap4A
mutant enzyme K36M
Caenorhabditis elegans
12
-
Ap4A
mutant enzyme H31A
Caenorhabditis elegans
14
-
Ap4A
mutant enzyme H31V; mutant enzyme Y121A
Caenorhabditis elegans
23
-
Ap4A
wild-type enzyme
Caenorhabditis elegans
26
-
Ap4A
mutant enzyme Y27A
Caenorhabditis elegans
29
-
Ap4A
mutant enzyme Y27D
Caenorhabditis elegans
30
-
Ap4A
mutant enzyme K81M
Caenorhabditis elegans
31
-
Ap4A
mutant enzyme H38G; mutant enzyme H38K
Caenorhabditis elegans
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli, mutant enzymes Y27A, Y27D, H31A, H31V, W32G, K36M, H38G, H38K, E52Q, E56Q, Y76A, Y76/Y121A, K79M, K81M, K83M, E103Q, Y121A
Caenorhabditis elegans
Engineering (protein specific)
Protein Variants
Commentary
Organism
E103Q
turnover-number for hydrolysis of Ap4A is 3.2% of that of the wild-type enzyme, KM-value is 66% of the wild-type value
Caenorhabditis elegans
E52Q
turnover-number for hydrolysis of Ap4A is 0.02% of that of the wild-type enzyme, KM-value is 60% of the wild-type value
Caenorhabditis elegans
E56Q
turnover-number for hydrolysis of Ap4A is 0.001% of that of the wild-type enzyme, KM-value is 90% of the wild-type value
Caenorhabditis elegans
H31A
turnover-number for hydrolysis of Ap4A is 52% of that of the wild-type enzyme, KM-value is 8.3fold higher than the KM-value of the wild-type enzyme
Caenorhabditis elegans
H31V
turnover-number for hydrolysis of Ap4A is 61% of that of the wild-type enzyme, KM-value is 12.5fold higher than the KM-value of the wild-type enzyme
Caenorhabditis elegans
H38G
turnover-number for hydrolysis of Ap4A is 135% of that of the wild-type enzyme, KM-value is 66% of the wild-type value
Caenorhabditis elegans
H38K
turnover-number for hydrolysis of Ap4A is 135% of that of the wild-type enzyme, KM-value is 47% of the wild-type value
Caenorhabditis elegans
K36M
turnover-number for hydrolysis of Ap4A is 9% of that of the wild-type enzyme, KM-value is 1.5fold higher than the KM-value of the wild-type enzyme
Caenorhabditis elegans
K79M
turnover-number for hydrolysis of Ap4A is 0.7% of that of the wild-type enzyme, KM-value is 1.7fold higher than the KM-value of the wild-type enzyme
Caenorhabditis elegans
K81M
turnover-number for hydrolysis of Ap4A is 130% of that of the wild-type enzyme, KM-value is 2.3fold higher than the KM-value of the wild-type enzyme
Caenorhabditis elegans
K83M
turnover-number for hydrolysis of Ap4A is 2.6% of that of the wild-type enzyme, KM-value is 15.9fold higher than the KM-value of the wild-type enzyme
Caenorhabditis elegans
Y121A
turnover-number for hydrolysis of Ap4A is 61% of that of the wild-type enzyme, KM-value is 8.5fold higher than the KM-value of the wild-type enzyme
Caenorhabditis elegans
Y27A
turnover-number for hydrolysis of Ap4A is 113% of that of the wild-type enzyme, KM-value is 1.25fold higher than the KM-value of the wild-type enzyme
Caenorhabditis elegans
Y27D
turnover-number for hydrolysis of Ap4A is 126% of that of the wild-type enzyme, KM-value is 1.8fold higher than the KM-value of the wild-type enzyme
Caenorhabditis elegans
Y76A
turnover-number for hydrolysis of Ap4A is 8.7% of that of the wild-type enzyme, KM-value is 6.7fold higher than the KM-value of the wild-type enzyme
Caenorhabditis elegans
Y76A/Y121A
turnover-number for hydrolysis of Ap4A is 4.8% of that of the wild-type enzyme, KM-value is 3.75fold higher than the KM-value of the wild-type enzyme
Caenorhabditis elegans
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0041
-
Ap4A
mutant enzyme H38K
Caenorhabditis elegans
0.0053
-
Ap4A
mutant enzyme E52Q
Caenorhabditis elegans
0.0058
-
Ap4A
mutant enzyme E103Q; mutant enzyme H38G
Caenorhabditis elegans
0.0079
-
Ap4A
mutant enzyme E56Q
Caenorhabditis elegans
0.0088
-
Ap4A
wild-type enzyme
Caenorhabditis elegans
0.011
-
Ap4A
mutant enzyme Y27A
Caenorhabditis elegans
0.013
-
Ap4A
mutant enzyme K36M
Caenorhabditis elegans
0.015
-
Ap4A
mutant enzyme K79M
Caenorhabditis elegans
0.016
-
Ap4A
mutant enzyme Y27D
Caenorhabditis elegans
0.02
-
Ap4A
mutant enzyme K81M
Caenorhabditis elegans
0.033
-
Ap4A
mutant enzyme Y76A/Y121A
Caenorhabditis elegans
0.059
-
Ap4A
mutant enzyme Y76A
Caenorhabditis elegans
0.073
-
Ap4A
mutant enzyme H31A
Caenorhabditis elegans
0.075
-
Ap4A
mutant enzyme Y121A
Caenorhabditis elegans
0.11
-
Ap4A
mutant enzyme H31V
Caenorhabditis elegans
0.14
-
Ap4A
mutant enzyme K83M
Caenorhabditis elegans
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
diadenosine 5',5''-P1,P4-tetraphosphate + H2O
-
656173
Caenorhabditis elegans
ATP + AMP
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.00024
-
Ap4A
mutant enzyme E56Q
Caenorhabditis elegans
0.0052
-
Ap4A
mutant enzyme E52Q
Caenorhabditis elegans
0.16
-
Ap4A
mutant enzyme K79M
Caenorhabditis elegans
0.6
-
Ap4A
mutant enzyme K83M
Caenorhabditis elegans
0.75
-
Ap4A
mutant enzyme E103Q
Caenorhabditis elegans
1.1
-
Ap4A
mutant enzyme Y76A/Y121A
Caenorhabditis elegans
2
-
Ap4A
mutant enzyme Y76A
Caenorhabditis elegans
2.1
-
Ap4A
mutant enzyme K36M
Caenorhabditis elegans
12
-
Ap4A
mutant enzyme H31A
Caenorhabditis elegans
14
-
Ap4A
mutant enzyme H31V; mutant enzyme Y121A
Caenorhabditis elegans
23
-
Ap4A
wild-type enzyme
Caenorhabditis elegans
26
-
Ap4A
mutant enzyme Y27A
Caenorhabditis elegans
29
-
Ap4A
mutant enzyme Y27D
Caenorhabditis elegans
30
-
Ap4A
mutant enzyme K81M
Caenorhabditis elegans
31
-
Ap4A
mutant enzyme H38G; mutant enzyme H38K
Caenorhabditis elegans
Other publictions for EC 3.6.1.17
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
Synonyms
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)
733091
Wu
Elucidating diphosphoinositol ...
Homo sapiens
Angew. Chem. Int. Ed. Engl.
53
7192-7197
2014
-
-
-
-
-
-
3
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
3
3
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
733346
Barta
Chlamydia trachomatis CT771 (n ...
Chlamydia trachomatis
Biochemistry
53
214-224
2014
-
-
-
1
-
-
-
6
-
2
-
-
-
6
-
-
-
-
-
-
-
-
1
-
2
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
6
-
2
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
6
-
-
-
-
-
-
-
-
6
6
733872
Sasaki
Enzymatic characteristics of a ...
Myxococcus xanthus, Myxococcus xanthus DK 1622
FEBS Lett.
588
3395-3402
2014
-
-
-
-
-
-
5
2
-
2
-
-
-
2
-
-
-
-
-
-
-
-
6
-
2
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
5
-
2
-
2
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
2
-
-
-
-
-
-
-
-
2
2
733257
Ge
Crystal structure of wild-type ...
Homo sapiens
Biochem. Biophys. Res. Commun.
432
16-21
2013
-
-
-
1
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
733450
Osman
Molecular characterization and ...
Plasmodium falciparum
Biol. Pharm. Bull.
35
1191-1196
2012
-
-
1
-
2
-
-
3
-
5
1
-
-
4
-
-
-
-
-
-
-
-
2
1
1
1
-
1
3
1
-
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
3
-
5
1
-
-
-
-
-
-
-
-
-
2
1
1
-
1
3
1
-
-
-
-
-
-
-
-
-
733563
Albright
NPP4 is a procoagulant enzyme ...
Homo sapiens
Blood
120
4432-4440
2012
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
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-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
719339
Arczewska
Caenorhabditis elegans NDX-4 i ...
Caenorhabditis elegans, Caenorhabditis elegans Bristol N2
DNA Repair
10
176-187
2011
-
-
1
-
-
-
-
5
-
-
-
-
-
6
-
-
1
-
-
-
-
-
10
-
1
-
-
-
5
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
1
-
-
-
-
10
-
-
-
-
5
-
-
-
-
-
2
2
-
5
5
710715
Jeyakanthan
Free and ATP-bound structures ...
Aquifex aeolicus
Acta Crystallogr. Sect. D
66
116-124
2010
-
-
1
1
-
-
-
3
-
-
-
-
-
3
-
-
1
-
-
-
-
-
3
-
4
-
-
-
3
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
3
-
-
-
-
-
-
-
1
-
-
-
-
3
-
-
-
-
3
-
-
-
-
-
-
-
-
3
3
713580
Vasilenko
SARS coronavirus protein 7a in ...
Homo sapiens
Virol. J.
7
31
2010
-
-
-
-
-
-
-
-
1
-
-
1
-
4
-
-
-
-
-
1
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
697896
Guranowski
Novel diadenosine polyphosphat ...
Homo sapiens, Lupinus angustifolius
FEBS J.
276
1546-1553
2009
-
-
-
-
-
-
4
2
-
2
-
2
-
4
-
-
1
-
-
-
-
-
6
-
4
2
-
-
-
2
-
-
-
4
-
-
-
-
-
-
-
-
-
-
4
4
2
-
2
-
2
-
-
-
1
-
-
-
-
6
-
2
-
-
-
2
-
-
-
-
-
-
-
-
-
711209
Branson
Discovery of inhibitors of lup ...
Lupinus angustifolius
Biochemistry
48
7614-7620
2009
-
-
-
-
-
-
7
-
-
-
-
-
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1
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Nuclear location of a diadenos ...
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Lazewska
Human placental (asymmetrical) ...
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Robinson
Isolation and charcterization ...
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Dinucleoside tetraphosphatase ...
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Cameselle
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Dinucleosidasetetraphosphatase ...
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Vallejo
Diguanosinetetraphosphate guan ...
Artemia salina
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209893
Warner
Isolation, purification, and c ...
Artemia salina
Biochemistry
4
1568-1575
1965
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