Information on EC 3.1.3.27 - phosphatidylglycerophosphatase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

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EC NUMBER
COMMENTARY hide
3.1.3.27
-
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RECOMMENDED NAME
GeneOntology No.
phosphatidylglycerophosphatase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
phosphatidylglycerophosphate + H2O = phosphatidylglycerol + phosphate
show the reaction diagram
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
cardiolipin biosynthesis I
-
-
cardiolipin biosynthesis II
-
-
cardiolipin biosynthesis III
-
-
phosphatidylglycerol biosynthesis I (plastidic)
-
-
phosphatidylglycerol biosynthesis II (non-plastidic)
-
-
type I lipoteichoic acid biosynthesis (S. aureus)
-
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cardiolipin biosynthesis
-
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lipid metabolism
-
-
Glycerophospholipid metabolism
-
-
Metabolic pathways
-
-
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SYSTEMATIC NAME
IUBMB Comments
phosphatidylglycerophosphate phosphohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9033-46-9
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
Escherichia coli B / ATCC 11303
-
C6EFV6
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Syrian hamster
-
-
Manually annotated by BRENDA team
Micrococcus cerificans
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
baker´s yeast
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
phosphatidylglycerophosphate phosphatase essential for the biosynthesis of cardiolipin, an integral component of mitochondrial and bacterial membranes
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,2-dioctanoyl-sn-glycero-3-diphosphate + H2O
?
show the reaction diagram
1,2-dioleoyl-sn-glycero-3-diphosphate + H2O
?
show the reaction diagram
1,2-dioleoyl-sn-glycero-3-phosphate + H2O
1,2-dioleoyl-sn-glycerol + phosphate
show the reaction diagram
1-oleoyl-2-lyso-sn-glycero-3-phosphate + H2O
1-oleoyl-2-lyso-sn-glycerol + phosphate
show the reaction diagram
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
dipalmitoyl sn-glycero 3-phosphate + H2O
dipalmitoyl sn-glycerol + phosphate
show the reaction diagram
-
-
-
r
phosphatidylglycerol 3-phosphate + H2O
phosphatidylglycerol + phosphate
show the reaction diagram
phosphatidylglycerophosphate + H2O
?
show the reaction diagram
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
show the reaction diagram
sn-phosphatidyl 1-sn-glycero 3-phosphate + H2O
3-phosphatidylglycerol + phosphate
show the reaction diagram
-
-
-
?
undecaprenyl diphosphate + H2O
?
show the reaction diagram
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
phosphatidylglycerophosphate + H2O
?
show the reaction diagram
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
show the reaction diagram
-
-
-
-
?
undecaprenyl diphosphate + H2O
?
show the reaction diagram
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
each protomer contains an independent active site with two metal ions, Ca2+ and Mg2+, forming a heterobinuclear center located in a hydrophilic cavity near the surface of the molecule
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
-
-
EDTA
-
higher concentrations
iodoacetamide
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-
ionic and non-ionic detergents
-
most effective is Triton X-100
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Mg2+
-
-
N-ethylmaleimide
-
-
Octadecylamine
-
-
octyl-beta-D-glucopyranoside
-
complete inhibition with 30 mM
oleic acid
-
higher than 1.5 mM
p-Chloromercuriphenylsulfonic acid
-
100% inhibition at 1 mM
p-mercuribenzoic acid
-
-
phosphate
phosphatidic acid ammonium salt
-
3.0 mM
phosphatidylglycerophosphate
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more than 100 æM
Sulfhydryl inhibitors
-
-
-
trimethyloctadecyl ammonium chloride
-
-
Triton X-100
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
arachidonic acid
-
-
EGTA
-
0.01 - 0.10 mM
oleic acid
-
1.9 fold stimulation at 0.5 mM
phosphatidic acid sodium salt
-
2 fold stimulation at 3.0 mM
Triton X-100
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3
1,2-dioleoyl-sn-glycero-3-phosphate
C6EFV6;
pH and temperature not specified in the publication
0.012
dipalmitoyl sn-glycero 3-phosphate
-
-
0.002 - 0.18
phosphatidylglycerophosphate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
24
1,2-dioleoyl-sn-glycero-3-phosphate
C6EFV6;
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0004
-
-
0.0017
-
partially purified
0.0018
-
pgpB geneproduct
0.0021
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pgpA geneproduct
0.0023
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partially purified
0.01
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PGP-C
0.014
-
compound of PGP-A,-B and -C
0.028
-
partially purified
0.13
-
PGP-B and -C
0.19
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PGP-A and -C
5.2
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PGPC-tase
6
-
PGPA-tase, more specific for phosphatidylglycerolphosphate than PGPB-tase
10.1
-
PGPB-tase
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3
-
-
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
-
little activity below pH 7.0 and above pH 8.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Bacillus subtilis (strain 168);
A0A140N9T3
Escherichia coli (strain B / BL21-DE3);
P0A924
Escherichia coli (strain K12);
Mus musculus;
Neisseria meningitidis serogroup B (strain MC58);
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
C6EFV6;
x * 29000, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
-
x-ray crystallography
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
vapor diffusion method
C6EFV6;
with precipitant containing 30% pentaerythritol ethoxylate, 50 mM ammonium sulfate, 50 mM Bis-Tris at pH 6.5
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
95% activity for several weeks, stored in liquid nitrogen
94818
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43
C6EFV6;
the melting temperature of the wild type enzyme is 43°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
50% loss of activity after solubilization with Triton X-100 in 12 h
-
heat labile
heat stable up to 50°C
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inactivation above 60°C
-
PGP-C more sensitive to increasing temperature
presence of dithiothreitol required
-
resistant to solubilization with Triton X-100 if 5 mM EDTA is included
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sensitive to sulfhydryl reagents and freeze-thaw cycles
the enzyme is stabilized by Na2MoO4 but not by Na2SO4
C6EFV6;
unstable at room temperature
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Triton X-100
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-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable for several months in 0.25 sucrose, 0.1 mM EDTA, pH 7.4
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-20°C, stable for weeks
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4°C, for weeks in 2% Triton X-100, 50 mM MgCl2, 20% glycerol, 0.5 M KCl
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4°C, stable for a number of weeks in 20% glycerol, 0.01 M Tris-HCl, pH 7.5, 0.1 mM EDTA, 50 mM beta-mercaptoethanol
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GST-bind resin column chromatography
-
partial
purified in a detergent combination of nonyl-beta-D-glucopyranoside and n-dodecyl-N,N-dimethylamine-N-oxide
C6EFV6;
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Escherichia coli strains lacking the original pgpA and/or pgpB genes
-
expressed in Escherichia coli
C6EFV6;
expressed in Escherichia coli BL21 (DE3) cells
-
expressed in Escherichia coli BL21 (DE3) CodonPlus RIPL cells
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A83F
C6EFV6;
the mutant shows reduced activity
D211E
C6EFV6;
the mutant shows strongly reduced activity
F61W
C6EFV6;
the mutant shows reduced activity
G89L
C6EFV6;
the mutant shows strongly reduced activity
G91M
C6EFV6;
the mutant shows reduced activity
H163A
C6EFV6;
the mutant shows strongly reduced activity
H207A
C6EFV6;
the mutant shows strongly reduced activity
H57F
C6EFV6;
the mutant shows about wild type activity
K93E
C6EFV6;
the mutant shows reduced activity
K97A
C6EFV6;
the mutant shows strongly reduced activity
L58F
C6EFV6;
the mutant shows about wild type activity
Q90A
C6EFV6;
the mutant shows reduced activity
R104A
C6EFV6;
the mutant shows strongly reduced activity
R201A
C6EFV6;
the mutant shows strongly reduced activity
V54F
C6EFV6;
the mutant shows reduced activity
V88F
C6EFV6;
the mutant shows reduced activity
H163A
Escherichia coli B / ATCC 11303
-
the mutant shows strongly reduced activity
-
H207A
Escherichia coli B / ATCC 11303
-
the mutant shows strongly reduced activity
-
K97A
Escherichia coli B / ATCC 11303
-
the mutant shows strongly reduced activity
-
R104A
Escherichia coli B / ATCC 11303
-
the mutant shows strongly reduced activity
-
R201A
Escherichia coli B / ATCC 11303
-
the mutant shows strongly reduced activity
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
-
preparation of phosphatidylglycerophosphate
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LINKS TO OTHER DATABASES (specific for EC-Number 3.1.3.27)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)