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show all sequences of 3.6.1.67

Structure and function of the E. coli dihydroneopterin triphosphate pyrophosphatase: a Nudix enzyme involved in folate biosynthesis

Gabelli, S.B.; Bianchet, M.A.; Xu, W.; Dunn, C.A.; Niu, Z.D.; Amzel, L.M.; Bessman, M.J.; Structure 15, 1014-1022 (2007)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
crystal structure resolved to 1.8 A resolution; the structure of the enzyme is determined by X-ray diffraction, 1.8 A resolution. The best crystals grow by microseeding in sitting-drop experiments with a 1 ml reservoir solution of 1.31.5 M ammonium sulfate, 1% propanol, 35 mM DTT, 4 mM sodium diphosphate, 100 mM Na HEPES (pH 6.8). Crystals belong to monoclinic space group C2 with cell dimensions a = 124.1 A, b = 43.2 A, c = 108.0 A, and b = 115.0
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.27
-
7,8-dihydroneopterin 3'-triphosphate
pH 8.5, 37C
Escherichia coli
0.79
-
dATP
pH 8.5, 37C
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
7,8-dihydroneopterin 3'-triphosphate + H2O
Escherichia coli
committed step of folate synthesis in bacteria
7,8-dihydroneopterin 3'-phosphate + diphosphate
-
-
?
7,8-dihydroneopterin 3'-triphosphate + H2O
Escherichia coli
key enzyme in the folate pathway
7,8-dihydroneopterin 3'-phosphate + diphosphate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
P0AFC0
-
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
3
8
pH 8.5, 37C
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
7,8-dihydroneopterin 3'-triphosphate + H2O
-
728808
Escherichia coli
7,8-dihydroneopterin 3'-phosphate + diphosphate
-
-
-
?
7,8-dihydroneopterin 3'-triphosphate + H2O
committed step of folate synthesis in bacteria
728808
Escherichia coli
7,8-dihydroneopterin 3'-phosphate + diphosphate
-
-
-
?
7,8-dihydroneopterin 3'-triphosphate + H2O
key enzyme in the folate pathway
728808
Escherichia coli
7,8-dihydroneopterin 3'-phosphate + diphosphate
-
-
-
?
dATP + H2O
-
728808
Escherichia coli
dAMP + diphosphate
-
-
-
?
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Escherichia coli
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4.59
-
dATP
pH 8.5, 37C
Escherichia coli
11.6
-
7,8-dihydroneopterin 3'-triphosphate
pH 8.5, 37C
Escherichia coli
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
assay at
Escherichia coli
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystal structure resolved to 1.8 A resolution; the structure of the enzyme is determined by X-ray diffraction, 1.8 A resolution. The best crystals grow by microseeding in sitting-drop experiments with a 1 ml reservoir solution of 1.31.5 M ammonium sulfate, 1% propanol, 35 mM DTT, 4 mM sodium diphosphate, 100 mM Na HEPES (pH 6.8). Crystals belong to monoclinic space group C2 with cell dimensions a = 124.1 A, b = 43.2 A, c = 108.0 A, and b = 115.0
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.27
-
7,8-dihydroneopterin 3'-triphosphate
pH 8.5, 37C
Escherichia coli
0.79
-
dATP
pH 8.5, 37C
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
7,8-dihydroneopterin 3'-triphosphate + H2O
Escherichia coli
committed step of folate synthesis in bacteria
7,8-dihydroneopterin 3'-phosphate + diphosphate
-
-
?
7,8-dihydroneopterin 3'-triphosphate + H2O
Escherichia coli
key enzyme in the folate pathway
7,8-dihydroneopterin 3'-phosphate + diphosphate
-
-
?
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
3
8
pH 8.5, 37C
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
7,8-dihydroneopterin 3'-triphosphate + H2O
-
728808
Escherichia coli
7,8-dihydroneopterin 3'-phosphate + diphosphate
-
-
-
?
7,8-dihydroneopterin 3'-triphosphate + H2O
committed step of folate synthesis in bacteria
728808
Escherichia coli
7,8-dihydroneopterin 3'-phosphate + diphosphate
-
-
-
?
7,8-dihydroneopterin 3'-triphosphate + H2O
key enzyme in the folate pathway
728808
Escherichia coli
7,8-dihydroneopterin 3'-phosphate + diphosphate
-
-
-
?
dATP + H2O
-
728808
Escherichia coli
dAMP + diphosphate
-
-
-
?
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Escherichia coli
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4.59
-
dATP
pH 8.5, 37C
Escherichia coli
11.6
-
7,8-dihydroneopterin 3'-triphosphate
pH 8.5, 37C
Escherichia coli
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
assay at
Escherichia coli
General Information
General Information
Commentary
Organism
malfunction
knockout of this gene in Escherichia coli leads to a marked reduction in folate synthesis that is completely restored by a plasmid carrying the gene
Escherichia coli
metabolism
metabolism
Escherichia coli
physiological function
committed step of folate synthesis in bacteria
Escherichia coli
General Information (protein specific)
General Information
Commentary
Organism
malfunction
knockout of this gene in Escherichia coli leads to a marked reduction in folate synthesis that is completely restored by a plasmid carrying the gene
Escherichia coli
metabolism
metabolism
Escherichia coli
physiological function
committed step of folate synthesis in bacteria
Escherichia coli
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
5.8
-
dATP
pH 8.5, 37C
Escherichia coli
43
-
7,8-dihydroneopterin 3'-triphosphate
pH 8.5, 37C
Escherichia coli
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
5.8
-
dATP
pH 8.5, 37C
Escherichia coli
43
-
7,8-dihydroneopterin 3'-triphosphate
pH 8.5, 37C
Escherichia coli
Other publictions for EC 3.6.1.67
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)
728808
Gabelli
Structure and function of the ...
Escherichia coli
Structure
15
1014-1022
2007
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4
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1
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1
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1
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2
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1
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4
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1
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2
1
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3
3
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2
2
727354
Hori
Dual hydrolysis of diphosphate ...
Escherichia coli
DNA Repair
4
33-39
2005
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2
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1
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727852
Klaus
A nudix enzyme removes pyropho ...
Arabidopsis thaliana, Lactococcus lactis, Lactococcus lactis NZ9000
J. Biol. Chem.
280
5274-5280
2004
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2
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3
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2
4
2
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7
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1
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2
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8
2
2
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3
2
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2
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3
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2
4
2
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1
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2
-
8
2
2
-
-
3
2
-
-
-
-
1
1
-
3
3
729956
OHandley
Escherichia coli orf17 codes f ...
Escherichia coli
J. Biol. Chem.
271
24649-24654
1996
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1
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2
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1
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1
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727800
Suzuki
The biosynthesis of folic acid ...
Escherichia coli
J. Biol. Chem.
249
2405-2410
1974
-
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5
1
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1
1
1
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2
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1
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4
-
1
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2
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1
1
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6
-
2
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2
2
1
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2
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4
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2
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2
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2
2
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1
1
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