BRENDA - Enzyme Database show
show all sequences of 5.1.99.7

Purification, cloning, and functional expression of dihydroneopterin triphosphate 2'-epimerase from Escherichia coli

Ahn, C.; Byun, J.; Yim, J.; J. Biol. Chem. 272, 15323-15328 (1997)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
DNA and amino acid sequence determination and analysis
Escherichia coli
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
13700
-
6 * 13700, SDS-PAGE, 6 * 13993, sequence calculation
Escherichia coli
13993
-
6 * 13700, SDS-PAGE, 6 * 13993, sequence calculation
Escherichia coli
82600
-
gel filtration
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
Escherichia coli
-
7,8-dihydromonapterin 3'-triphosphate
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
P0AC19
-
-
Purification (Commentary)
Commentary
Organism
native enzyme 954fold by ammonium sulfate fractionation, Cibacron blue 3GA affinity chromatography, hydrophobic interaction chromatography, methotrexate affinity chromatography, and ge filtration, to homogeneity
Escherichia coli
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
505
-
purified native enzyme, substrate 7,8-dihydroneopterin 3'-triphosphate, pH 6.2, 50C
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
-
734122
Escherichia coli
7,8-dihydromonapterin 3'-triphosphate
-
-
-
r
Subunits
Subunits
Commentary
Organism
homohexamer
6 * 13700, SDS-PAGE, 6 * 13993, sequence calculation
Escherichia coli
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
50
-
assay at
Escherichia coli
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.2
-
assay at
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
DNA and amino acid sequence determination and analysis
Escherichia coli
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
13700
-
6 * 13700, SDS-PAGE, 6 * 13993, sequence calculation
Escherichia coli
13993
-
6 * 13700, SDS-PAGE, 6 * 13993, sequence calculation
Escherichia coli
82600
-
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
7,8-dihydroneopterin 3'-triphosphate
Escherichia coli
-
7,8-dihydromonapterin 3'-triphosphate
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
native enzyme 954fold by ammonium sulfate fractionation, Cibacron blue 3GA affinity chromatography, hydrophobic interaction chromatography, methotrexate affinity chromatography, and ge filtration, to homogeneity
Escherichia coli
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
505
-
purified native enzyme, substrate 7,8-dihydroneopterin 3'-triphosphate, pH 6.2, 50C
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
-
734122
Escherichia coli
7,8-dihydromonapterin 3'-triphosphate
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
homohexamer
6 * 13700, SDS-PAGE, 6 * 13993, sequence calculation
Escherichia coli
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
50
-
assay at
Escherichia coli
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.2
-
assay at
Escherichia coli
General Information
General Information
Commentary
Organism
metabolism
in Escherichia coli, L-monapterin is made from dihydromonapterin triphosphate after successive dephosphorylation and oxidation. Dihydromonapterin triphosphate is formed by an epimerase acting on C2' carbon of dihydroneopterin triphosphate, which is made from GTP by GTP cyclohydrolase I (EC 3.5.4.16)
Escherichia coli
General Information (protein specific)
General Information
Commentary
Organism
metabolism
in Escherichia coli, L-monapterin is made from dihydromonapterin triphosphate after successive dephosphorylation and oxidation. Dihydromonapterin triphosphate is formed by an epimerase acting on C2' carbon of dihydroneopterin triphosphate, which is made from GTP by GTP cyclohydrolase I (EC 3.5.4.16)
Escherichia coli
Other publictions for EC 5.1.99.7
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)
733859
Gabrielsen
FolX from Pseudomonas aerugino ...
Pseudomonas aeruginosa
FEBS Lett.
586
1160-1165
2012
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1
1
1
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1
1
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1
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1
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1
1
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1
1
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1
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1
1
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1
-
-
-
-
1
1
-
-
-
-
-
-
-
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2
2
-
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-
704330
Pribat
FolX and FolM are essential fo ...
Escherichia coli, Pseudomonas aeruginosa
J. Bacteriol.
192
475-482
2010
-
-
2
-
2
-
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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
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2
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2
-
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-
-
-
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3
3
-
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5109
Haumann
Biosynthesis of pteridines in ...
Escherichia coli, Escherichia coli XL1-Blue
J. Biol. Chem.
273
17418-17424
1998
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1
-
1
-
1
4
-
-
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1
-
7
-
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1
1
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1
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3
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1
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1
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1
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1
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1
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4
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1
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1
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1
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3
-
1
-
-
-
1
-
-
-
-
2
2
-
-
-
734122
Ahn
Purification, cloning, and fun ...
Escherichia coli
J. Biol. Chem.
272
15323-15328
1997
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1
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3
1
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2
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1
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1
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1
1
1
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1
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1
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3
1
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1
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1
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1
1
1
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1
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1
1
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