BRENDA - Enzyme Database show
show all sequences of 3.6.1.27

Substrate specificity and membrane topology of Escherichia coli PgpB, an undecaprenyl pyrophosphate phosphatase

Touze, T.; Blanot, D.; Mengin-Lecreulx, D.; J. Biol. Chem. 283, 16573-16583 (2008)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
cardiolipin
-
Escherichia coli
diacylglycerol diphosphate
increases the activity with undecaprenyl diphosphate by about 400%
Escherichia coli
phosphatidylglycerol
-
Escherichia coli
Phospholipids
-
Escherichia coli
Cloned(Commentary)
Commentary
Organism
gene pgpB, overexpression of His-tagged enzyme in strain DH5alpha and C43
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.08
-
diacylglycerol diphosphate
pH 7.5, 37°C, recombinant enzyme
Escherichia coli
0.096
-
farnesyl diphosphate
pH 7.5, 37°C, recombinant enzyme
Escherichia coli
0.53
-
undecaprenyl diphosphate
pH 7.5, 37°C, recombinant enzyme
Escherichia coli
1.7
-
phosphatidic acid
pH 7.5, 37°C, recombinant enzyme
Escherichia coli
3.6
-
isopentenyl diphosphate
pH 7.5, 37°C, recombinant enzyme
Escherichia coli
3.9
-
diphosphate
pH 7.5, 37°C, recombinant enzyme
Escherichia coli
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
integral, PgpB contains six transmembrane segments, a large periplasmic loop, and the type 2 phosphatidic acid phosphatase signature residues at a periplasmic location
Escherichia coli
16020
-
additional information
topological mapping, modelling, overview
Escherichia coli
-
-
periplasm
PgpB contains six transmembrane segments, a large periplasmic loop, and the type 2 phosphatidic acid phosphatase signature residues at a periplasmic location
Escherichia coli
-
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
30000
-
x * 30158, mass spectrometry, x * 30000, SDS-PAGE
Escherichia coli
30158
-
x * 30158, mass spectrometry, x * 30000, SDS-PAGE
Escherichia coli
110000
-
recombinant His-tagged enzyme, gel filtration
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
undecaprenyl diphosphate + H2O
Escherichia coli
the synthesis of the lipid carrier undecaprenyl phosphate, C55-P, requires the dephosphorylation of its precursor, undecaprenyl pyrophosphate, C55-PP, the dephosphorylation involves four integral membrane proteins, BacA, and three members of the type 2 phosphatidic acid phosphatase family, PgpB, YbjG, and YeiU, overview
undecaprenyl phosphate + phosphate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged enzyme from membranes to homogeneity by ultracentrifugation, nickel affinity chromatography
Escherichia coli
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1
-
purified recombinant enzyme, substrate isopentenyl diphosphate
Escherichia coli
3
-
purified recombinant enzyme, substrate undecaprenyl diphosphate
Escherichia coli
6.7
-
purified recombinant enzyme, substrate phosphatidic acid
Escherichia coli
300
-
purified recombinant enzyme, substrate farnesyl diphosphate
Escherichia coli
310
-
purified recombinant enzyme, substrate diacylglycerol diphosphate
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
diacylglycerol diphosphate + H2O
-
687718
Escherichia coli
diacylglycerol phosphate + phosphate
-
-
-
?
diphosphate + H2O
low activity
687718
Escherichia coli
2 phosphate
-
-
-
?
farnesyl diphosphate + H2O
-
687718
Escherichia coli
farnesyl phosphate + phosphate
-
-
-
?
isopentenyl diphosphate + H2O
low activity
687718
Escherichia coli
isopentenyl phosphate + phosphate
-
-
-
?
additional information
substrate specificity, overview
687718
Escherichia coli
?
-
-
-
-
phosphatidic acid + H2O
low activity
687718
Escherichia coli
?
-
-
-
?
undecaprenyl diphosphate + H2O
low activity
687718
Escherichia coli
undecaprenyl phosphate + phosphate
-
-
-
?
undecaprenyl diphosphate + H2O
the synthesis of the lipid carrier undecaprenyl phosphate, C55-P, requires the dephosphorylation of its precursor, undecaprenyl pyrophosphate, C55-PP, the dephosphorylation involves four integral membrane proteins, BacA, and three members of the type 2 phosphatidic acid phosphatase family, PgpB, YbjG, and YeiU, overview
687718
Escherichia coli
undecaprenyl phosphate + phosphate
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
the enzyme exists as a monomer in n-dodecyl-beta-D-maltoside solution, topological mapping, overview
Escherichia coli
oligomer
x * 30158, mass spectrometry, x * 30000, SDS-PAGE
Escherichia coli
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
9
-
undecaprenyl diphosphate
pH 7.5, 37°C, recombinant enzyme
Escherichia coli
19
-
isopentenyl diphosphate
pH 7.5, 37°C, recombinant enzyme
Escherichia coli
48
-
diphosphate
pH 7.5, 37°C, recombinant enzyme
Escherichia coli
61
-
phosphatidic acid
pH 7.5, 37°C, recombinant enzyme
Escherichia coli
280
-
diacylglycerol diphosphate
pH 7.5, 37°C, recombinant enzyme
Escherichia coli
290
-
farnesyl diphosphate
pH 7.5, 37°C, recombinant enzyme
Escherichia coli
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
7.5
-
Escherichia coli
pH Range
pH Minimum
pH Maximum
Commentary
Organism
5
9
50% of maximal activity at pH values other than pH 6.5-pH 7.5
Escherichia coli
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
cardiolipin
-
Escherichia coli
diacylglycerol diphosphate
increases the activity with undecaprenyl diphosphate by about 400%
Escherichia coli
phosphatidylglycerol
-
Escherichia coli
Phospholipids
-
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
gene pgpB, overexpression of His-tagged enzyme in strain DH5alpha and C43
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.08
-
diacylglycerol diphosphate
pH 7.5, 37°C, recombinant enzyme
Escherichia coli
0.096
-
farnesyl diphosphate
pH 7.5, 37°C, recombinant enzyme
Escherichia coli
0.53
-
undecaprenyl diphosphate
pH 7.5, 37°C, recombinant enzyme
Escherichia coli
1.7
-
phosphatidic acid
pH 7.5, 37°C, recombinant enzyme
Escherichia coli
3.6
-
isopentenyl diphosphate
pH 7.5, 37°C, recombinant enzyme
Escherichia coli
3.9
-
diphosphate
pH 7.5, 37°C, recombinant enzyme
Escherichia coli
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
integral, PgpB contains six transmembrane segments, a large periplasmic loop, and the type 2 phosphatidic acid phosphatase signature residues at a periplasmic location
Escherichia coli
16020
-
additional information
topological mapping, modelling, overview
Escherichia coli
-
-
periplasm
PgpB contains six transmembrane segments, a large periplasmic loop, and the type 2 phosphatidic acid phosphatase signature residues at a periplasmic location
Escherichia coli
-
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
30000
-
x * 30158, mass spectrometry, x * 30000, SDS-PAGE
Escherichia coli
30158
-
x * 30158, mass spectrometry, x * 30000, SDS-PAGE
Escherichia coli
110000
-
recombinant His-tagged enzyme, 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
undecaprenyl diphosphate + H2O
Escherichia coli
the synthesis of the lipid carrier undecaprenyl phosphate, C55-P, requires the dephosphorylation of its precursor, undecaprenyl pyrophosphate, C55-PP, the dephosphorylation involves four integral membrane proteins, BacA, and three members of the type 2 phosphatidic acid phosphatase family, PgpB, YbjG, and YeiU, overview
undecaprenyl phosphate + phosphate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzyme from membranes to homogeneity by ultracentrifugation, nickel affinity chromatography
Escherichia coli
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1
-
purified recombinant enzyme, substrate isopentenyl diphosphate
Escherichia coli
3
-
purified recombinant enzyme, substrate undecaprenyl diphosphate
Escherichia coli
6.7
-
purified recombinant enzyme, substrate phosphatidic acid
Escherichia coli
300
-
purified recombinant enzyme, substrate farnesyl diphosphate
Escherichia coli
310
-
purified recombinant enzyme, substrate diacylglycerol diphosphate
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
diacylglycerol diphosphate + H2O
-
687718
Escherichia coli
diacylglycerol phosphate + phosphate
-
-
-
?
diphosphate + H2O
low activity
687718
Escherichia coli
2 phosphate
-
-
-
?
farnesyl diphosphate + H2O
-
687718
Escherichia coli
farnesyl phosphate + phosphate
-
-
-
?
isopentenyl diphosphate + H2O
low activity
687718
Escherichia coli
isopentenyl phosphate + phosphate
-
-
-
?
additional information
substrate specificity, overview
687718
Escherichia coli
?
-
-
-
-
phosphatidic acid + H2O
low activity
687718
Escherichia coli
?
-
-
-
?
undecaprenyl diphosphate + H2O
low activity
687718
Escherichia coli
undecaprenyl phosphate + phosphate
-
-
-
?
undecaprenyl diphosphate + H2O
the synthesis of the lipid carrier undecaprenyl phosphate, C55-P, requires the dephosphorylation of its precursor, undecaprenyl pyrophosphate, C55-PP, the dephosphorylation involves four integral membrane proteins, BacA, and three members of the type 2 phosphatidic acid phosphatase family, PgpB, YbjG, and YeiU, overview
687718
Escherichia coli
undecaprenyl phosphate + phosphate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
the enzyme exists as a monomer in n-dodecyl-beta-D-maltoside solution, topological mapping, overview
Escherichia coli
oligomer
x * 30158, mass spectrometry, x * 30000, SDS-PAGE
Escherichia coli
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
9
-
undecaprenyl diphosphate
pH 7.5, 37°C, recombinant enzyme
Escherichia coli
19
-
isopentenyl diphosphate
pH 7.5, 37°C, recombinant enzyme
Escherichia coli
48
-
diphosphate
pH 7.5, 37°C, recombinant enzyme
Escherichia coli
61
-
phosphatidic acid
pH 7.5, 37°C, recombinant enzyme
Escherichia coli
280
-
diacylglycerol diphosphate
pH 7.5, 37°C, recombinant enzyme
Escherichia coli
290
-
farnesyl diphosphate
pH 7.5, 37°C, recombinant enzyme
Escherichia coli
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
7.5
-
Escherichia coli
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
5
9
50% of maximal activity at pH values other than pH 6.5-pH 7.5
Escherichia coli
Other publictions for EC 3.6.1.27
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)
734263
Chang
Proposed carrier lipid-binding ...
Escherichia coli
J. Biol. Chem.
289
18719-18735
2014
-
-
1
-
17
-
2
1
-
2
1
-
-
2
-
-
-
-
-
-
-
-
1
1
-
-
-
1
1
-
-
-
1
-
1
-
-
1
-
-
17
-
1
2
1
1
-
2
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
1
1
-
-
-
-
-
-
-
-
-
734038
Shaaly
Undecaprenyl pyrophosphate pho ...
Enterococcus faecalis
J. Antimicrob. Chemother.
68
1583-1593
2013
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
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-
-
-
-
-
-
-
-
1
1
1
1
-
-
718534
Coker
-
Current understanding of de no ...
Bacillus subtilis, Escherichia coli
Afr. J. Microbiol. Res.
5
2555-2565
2011
-
-
-
-
-
-
-
-
2
-
-
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2
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2
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2
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-
-
2
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
718588
Hashizume
Tripropeptin C blocks the lipi ...
Micrococcus luteus
Antimicrob. Agents Chemother.
55
3821-3828
2011
-
-
-
-
-
-
2
-
1
-
-
-
-
1
-
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1
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1
2
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1
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-
-
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-
-
-
-
-
-
-
-
-
-
-
713052
Hynninen
An efflux transporter PbrA and ...
Cupriavidus metallidurans, Cupriavidus metallidurans CH34
Mol. Microbiol.
74
384-394
2009
-
-
1
-
-
-
2
-
1
-
-
-
-
9
-
-
1
-
-
-
-
-
12
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
1
-
-
-
-
12
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
687718
Touze
Substrate specificity and memb ...
Escherichia coli
J. Biol. Chem.
283
16573-16583
2008
4
-
1
-
-
-
-
6
3
-
3
1
-
2
-
-
1
-
-
-
5
-
8
2
1
-
-
6
1
1
-
-
-
-
-
4
-
1
-
-
-
-
-
-
-
6
3
-
3
1
-
-
-
1
-
-
5
-
8
2
1
-
-
6
1
1
-
-
-
-
-
-
-
-
688861
Tatar
An Escherichia coli undecapren ...
Escherichia coli
Microbiology
153
2518-2529
2007
-
-
-
-
1
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-
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2
-
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1
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2
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1
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2
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1
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2
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1
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1
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2
-
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-
-
-
-
-
-
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-
-
-
669336
El Ghachi
Identification of multiple gen ...
Escherichia coli
J. Biol. Chem.
280
18689-18695
2005
-
-
-
-
-
-
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-
-
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2
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1
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1
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-
-
-
-
-
-
-
-
-
669366
Bernard
BcrC from Bacillus subtilis ac ...
Bacillus subtilis
J. Biol. Chem.
280
28852-28857
2005
-
-
-
-
-
-
2
-
-
-
1
-
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4
-
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3
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2
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1
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3
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-
210607
Goldman
Purification and properties of ...
Micrococcus luteus
J. Biol. Chem.
247
5116-5122
1972
6
-
-
-
-
1
5
1
1
1
-
1
-
1
-
-
1
-
-
-
-
-
2
-
-
-
4
-
1
1
-
-
-
-
-
6
-
-
-
-
-
1
-
5
-
1
1
1
-
1
-
-
-
1
-
-
-
-
2
-
-
-
4
-
1
1
-
-
-
-
-
-
-
-
210606
Stone
Mechanism of action of bacitra ...
Enterococcus faecalis
Proc. Natl. Acad. Sci. USA
68
3223-3227
1971
-
-
-
-
-
-
1
-
1
9
-
1
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1
-
-
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-
-
-
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2
-
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1
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1
9
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1
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2
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