BRENDA - Enzyme Database
show all sequences of 3.6.1.67

The biosynthesis of folic acid. XII. Purification and properties of dihydroneopterin triphosphate pyrophosphohydrolase

Suzuki, Y.; Brown, G.M.; J. Biol. Chem. 249, 2405-2410 (1974)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
7,8-dihydroneopterin 3'-phosphate
0.074 mM, 21% inhibition; inhibits 21% at a concentration of 0.074 mM, when the substrate is present at 0.032 mM
Escherichia coli
diphosphate
1 mM, 89% inhibition
Escherichia coli
dTTP
1 mM, 72% inhibition
Escherichia coli
additional information
no inhibition by dihydrofolic acid, dihydropteroic acid, dihydroneopterin and 6-hydroxy-methyl-dihydropterin
Escherichia coli
TTP
1 mM, 72% inhibition
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.011
-
7,8-dihydroneopterin 3'-triphosphate
pH 8.5, 42C; pH 8.5, 42C
Escherichia coli
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
divalent cations are rerquired for the enzyme to function. Maximal activation is achieved with 8 mM Mg2+. Zn2+ and Ca2+ (both at 8 mM) are 2.4% and 7.1%, respectively, as effective as Mg2+. Mn2+ can not be tested because 7,8-dihydroneopterin triphosphate is rapidly and nonenzymatically decomposed in the presence of Mn2+; maximal activation is achieved with 8 nM Mg2+. Zn2+ and Ca2+ (both at 8 mM) are 2.4% and 7.1%, respectively, as effective as Mg2
Escherichia coli
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
17000
-
; gel filtration
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
7,8-dihydroneopterin 3'-triphosphate + H2O
Escherichia coli
the enzyme participates in a folate biosynthesis pathway
7,8-dihydroneopterin 3'-phosphate + diphosphate
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Escherichia coli
-
-
-
Escherichia coli
P0AFC0
-
-
Purification (Commentary)
Purification (Commentary)
Organism
partial; partial
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
7,8-dihydroneopterin 3'-triphosphate + H2O
-
727800
Escherichia coli
7,8-dihydroneopterin 3'-phosphate + diphosphate
-
-
-
?
7,8-dihydroneopterin 3'-triphosphate + H2O
the enzyme participates in a folate biosynthesis pathway
727800
Escherichia coli
7,8-dihydroneopterin 3'-phosphate + diphosphate
-
-
-
?
additional information
no activity with ATP, GTP, dihydroneopterin phosphate, 4-nitrophenyl hosphate or diphosphate
727800
Escherichia coli
?
-
-
-
-
Synonyms
Synonyms
Commentary
Organism
dihydroneopterin triphosphate pyrophosphohydrolase
-
Escherichia coli
H2-neopterin-PPP pyrophosphohydrolase
-
Escherichia coli
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
42
-
;
Escherichia coli
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
10
-
1 min, activity is destroyed
Escherichia coli
100
-
1 min, enzyme is destroyed
Escherichia coli
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
;
Escherichia coli
pH Range
pH Minimum
pH Maximum
Commentary
Organism
7.1
9.7
half-maximal activity at pH.1 and at pH 9.7; half-maximal activity at pH 7.1 and at pH 9.7
Escherichia coli
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
7,8-dihydroneopterin 3'-phosphate
0.074 mM, 21% inhibition
Escherichia coli
7,8-dihydroneopterin 3'-phosphate
inhibits 21% at a concentration of 0.074 mM, when the substrate is present at 0.032 mM
Escherichia coli
diphosphate
1 mM, 89% inhibition
Escherichia coli
dTTP
1 mM, 72% inhibition
Escherichia coli
additional information
no inhibition by dihydrofolic acid, dihydropteroic acid, dihydroneopterin and 6-hydroxy-methyl-dihydropterin
Escherichia coli
TTP
1 mM, 72% inhibition
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.011
-
7,8-dihydroneopterin 3'-triphosphate
pH 8.5, 42C
Escherichia coli
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
maximal activation is achieved with 8 nM Mg2+. Zn2+ and Ca2+ (both at 8 mM) are 2.4% and 7.1%, respectively, as effective as Mg2
Escherichia coli
Mg2+
divalent cations are rerquired for the enzyme to function. Maximal activation is achieved with 8 mM Mg2+. Zn2+ and Ca2+ (both at 8 mM) are 2.4% and 7.1%, respectively, as effective as Mg2+. Mn2+ can not be tested because 7,8-dihydroneopterin triphosphate is rapidly and nonenzymatically decomposed in the presence of Mn2+
Escherichia coli
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
17000
-
-
Escherichia coli
17000
-
gel filtration
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
7,8-dihydroneopterin 3'-triphosphate + H2O
Escherichia coli
the enzyme participates in a folate biosynthesis pathway
7,8-dihydroneopterin 3'-phosphate + diphosphate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
partial
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
7,8-dihydroneopterin 3'-triphosphate + H2O
-
727800
Escherichia coli
7,8-dihydroneopterin 3'-phosphate + diphosphate
-
-
-
?
7,8-dihydroneopterin 3'-triphosphate + H2O
the enzyme participates in a folate biosynthesis pathway
727800
Escherichia coli
7,8-dihydroneopterin 3'-phosphate + diphosphate
-
-
-
?
additional information
no activity with ATP, GTP, dihydroneopterin phosphate, 4-nitrophenyl hosphate or diphosphate
727800
Escherichia coli
?
-
-
-
-
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
42
-
-
Escherichia coli
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
10
-
1 min, activity is destroyed
Escherichia coli
100
-
1 min, enzyme is destroyed
Escherichia coli
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
-
Escherichia coli
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
7.1
9.7
half-maximal activity at pH 7.1 and at pH 9.7
Escherichia coli
7.1
9.7
half-maximal activity at pH.1 and at pH 9.7
Escherichia coli
General Information
General Information
Commentary
Organism
metabolism
the enzyme participates in a folate biosynthesis pathway
Escherichia coli
General Information (protein specific)
General Information
Commentary
Organism
metabolism
the enzyme participates in a folate biosynthesis pathway
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
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)
728808
Gabelli
Structure and function of the ...
Escherichia coli
Structure
15
1014-1022
2007
-
-
-
1
-
-
-
2
-
-
-
2
-
3
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1
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4
-
3
1
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2
1
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1
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2
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2
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-
-
-
1
-
4
-
1
-
-
2
1
-
-
-
-
3
3
-
2
2
727354
Hori
Dual hydrolysis of diphosphate ...
Escherichia coli
DNA Repair
4
33-39
2005
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
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-
-
1
-
1
-
-
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-
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1
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1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
727852
Klaus
A nudix enzyme removes pyropho ...
Arabidopsis thaliana, Lactococcus lactis, Lactococcus lactis NZ9000
J. Biol. Chem.
280
5274-5280
2004
-
-
2
-
-
-
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3
-
2
4
2
-
7
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1
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2
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8
2
10
2
-
-
3
2
-
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-
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-
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2
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-
-
-
-
-
-
3
-
2
4
2
-
-
-
1
-
-
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
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
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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
-
-
-
-
-
-
5
1
-
1
1
1
-
2
-
-
1
-
-
-
-
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4
-
4
1
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2
-
1
1
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-
6
-
2
-
2
2
1
-
-
-
2
-
-
-
-
4
-
2
-
2
-
2
2
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-
1
1
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-