BRENDA - Enzyme Database show
show all sequences of 5.1.99.7

FolX and FolM are essential for tetrahydromonapterin synthesis in Escherichia coli and Pseudomonas aeruginosa

Pribat, A.; Blaby, I.K.; Lara-Nunez, A.; Gregory, J.F.; de Crecy-Lagard, V.; Hanson, A.D.; J. Bacteriol. 192, 475-482 (2010)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene folX, genetic structure and phylogenetic analysis
Escherichia coli
gene folX, genetic structure and phylogenetic analysis
Pseudomonas aeruginosa
Engineering
Amino acid exchange
Commentary
Organism
additional information
construction of an Escherichia coli strain that lacks phenylalanine hydroxylase, PhhA, and in which the expression of Pseudomonas aeruginosa PhhA plus the recycling enzyme pterin 4a-carbinolamine dehydratase PhhB, rescues tyrosine auxotrophy. This rescue is abrogated by deleting folX or folM and restored by expressing the deleted gene from a plasmid. The folX deletion selectively eliminates tetrahydromonapterin production, the mutant strain lacks tetrahydromonapterin
Escherichia coli
additional information
deletion of tyrA (making PhhA the sole source of tyrosine) and folX results in a strain prototrophic for tyrosine, whereas the DELTAtyrA DELTAfolX strain is auxotrophic
Pseudomonas aeruginosa
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
7,8-dihydroneopterin 3'-triphosphate
Pseudomonas aeruginosa
-
7,8-dihydromonapterin 3'-triphosphate
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
gene folX
-
Pseudomonas aeruginosa
Q9HYG7
gene folX
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
7,8-dihydroneopterin 3'-triphosphate
-
704330
Escherichia coli
7,8-dihydromonapterin 3'-triphosphate
-
-
-
r
7,8-dihydroneopterin 3'-triphosphate
-
704330
Pseudomonas aeruginosa
7,8-dihydromonapterin 3'-triphosphate
-
-
-
r
Cloned(Commentary) (protein specific)
Commentary
Organism
gene folX, genetic structure and phylogenetic analysis
Escherichia coli
gene folX, genetic structure and phylogenetic analysis
Pseudomonas aeruginosa
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
construction of an Escherichia coli strain that lacks phenylalanine hydroxylase, PhhA, and in which the expression of Pseudomonas aeruginosa PhhA plus the recycling enzyme pterin 4a-carbinolamine dehydratase PhhB, rescues tyrosine auxotrophy. This rescue is abrogated by deleting folX or folM and restored by expressing the deleted gene from a plasmid. The folX deletion selectively eliminates tetrahydromonapterin production, the mutant strain lacks tetrahydromonapterin
Escherichia coli
additional information
deletion of tyrA (making PhhA the sole source of tyrosine) and folX results in a strain prototrophic for tyrosine, whereas the DELTAtyrA DELTAfolX strain is auxotrophic
Pseudomonas aeruginosa
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
7,8-dihydroneopterin 3'-triphosphate
Pseudomonas aeruginosa
-
7,8-dihydromonapterin 3'-triphosphate
-
-
r
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
-
704330
Escherichia coli
7,8-dihydromonapterin 3'-triphosphate
-
-
-
r
7,8-dihydroneopterin 3'-triphosphate
-
704330
Pseudomonas aeruginosa
7,8-dihydromonapterin 3'-triphosphate
-
-
-
r
General Information
General Information
Commentary
Organism
malfunction
deletion of gene folX selectively eliminates tetrahydromonapterin production
Escherichia coli
metabolism
tetrahydromonapterin formation requires both FolX and FolM, a dihydrofolate and dihydrobiopterin reductase. Tetrahydromonapterin is the physiological cofactor for phenylalanine hydroxylase, and tetrahydromonapterin can outrank folate as an end product of pterin biosynthesis, pterin pathway overview
Escherichia coli
metabolism
tetrahydromonapterin formation requires both FolX and FolM, a dihydrofolate and dihydrobiopterin reductase. Tetrahydromonapterin is the physiological cofactor for phenylalanine hydroxylase, and tetrahydromonapterin can outrank folate as an end product of pterin biosynthesis, pterin pathway overview
Pseudomonas aeruginosa
General Information (protein specific)
General Information
Commentary
Organism
malfunction
deletion of gene folX selectively eliminates tetrahydromonapterin production
Escherichia coli
metabolism
tetrahydromonapterin formation requires both FolX and FolM, a dihydrofolate and dihydrobiopterin reductase. Tetrahydromonapterin is the physiological cofactor for phenylalanine hydroxylase, and tetrahydromonapterin can outrank folate as an end product of pterin biosynthesis, pterin pathway overview
Escherichia coli
metabolism
tetrahydromonapterin formation requires both FolX and FolM, a dihydrofolate and dihydrobiopterin reductase. Tetrahydromonapterin is the physiological cofactor for phenylalanine hydroxylase, and tetrahydromonapterin can outrank folate as an end product of pterin biosynthesis, pterin pathway overview
Pseudomonas aeruginosa
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
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1
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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
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2
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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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3
3
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5109
HauŻmann
Biosynthesis of pteridines in ...
Escherichia coli, Escherichia coli XL1-Blue
J. Biol. Chem.
273
17418-17424
1998
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1
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1
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1
4
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1
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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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4
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1
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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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2
2
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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
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1
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