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Information on EC 3.1.3.27 - phosphatidylglycerophosphatase for references in articles please use BRENDA:EC3.1.3.27Word Map on EC 3.1.3.27
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Specify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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phosphatidylglycerophosphatase
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phosphatidylglycerophosphate + H2O = phosphatidylglycerol + phosphate
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hydrolysis of phosphoric ester
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cardiolipin biosynthesis I
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cardiolipin biosynthesis II
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cardiolipin biosynthesis III
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phosphatidylglycerol biosynthesis I (plastidic)
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phosphatidylglycerol biosynthesis II (non-plastidic)
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type I lipoteichoic acid biosynthesis (S. aureus)
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cardiolipin biosynthesis
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Glycerophospholipid metabolism
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phosphatidylglycerophosphate phosphohydrolase
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phosphatidylglycero phosphate phosphatase
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phosphatidylglycerophosphate phosphatase B
PGP phosphatase
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PGPase
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PgpB
C6EFV6;
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phosphatidylglycerophosphate phosphatase B
C6EFV6;
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phosphatidylglycerophosphate phosphatase B
C6EFV6;
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C6EFV6
UniProt
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Syrian hamster
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Micrococcus cerificans
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baker´s yeast
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C6EFV6
UniProt
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metabolism
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phosphatidylglycerophosphate phosphatase essential for the biosynthesis of cardiolipin, an integral component of mitochondrial and bacterial membranes
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1,2-dioctanoyl-sn-glycero-3-diphosphate + H2O
?
1,2-dioleoyl-sn-glycero-3-diphosphate + H2O
?
1,2-dioleoyl-sn-glycero-3-phosphate + H2O
1,2-dioleoyl-sn-glycerol + phosphate
1-oleoyl-2-lyso-sn-glycero-3-phosphate + H2O
1-oleoyl-2-lyso-sn-glycerol + phosphate
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
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?
dipalmitoyl sn-glycero 3-phosphate + H2O
dipalmitoyl sn-glycerol + phosphate
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r
phosphatidylglycerol 3-phosphate + H2O
phosphatidylglycerol + phosphate
phosphatidylglycerophosphate + H2O
?
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
sn-phosphatidyl 1-sn-glycero 3-phosphate + H2O
3-phosphatidylglycerol + phosphate
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?
undecaprenyl diphosphate + H2O
?
1,2-dioctanoyl-sn-glycero-3-diphosphate + H2O
?
C6EFV6;
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-
?
1,2-dioctanoyl-sn-glycero-3-diphosphate + H2O
?
C6EFV6;
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?
1,2-dioleoyl-sn-glycero-3-diphosphate + H2O
?
C6EFV6;
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?
1,2-dioleoyl-sn-glycero-3-diphosphate + H2O
?
C6EFV6;
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?
1,2-dioleoyl-sn-glycero-3-phosphate + H2O
1,2-dioleoyl-sn-glycerol + phosphate
C6EFV6;
highest activity
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?
1,2-dioleoyl-sn-glycero-3-phosphate + H2O
1,2-dioleoyl-sn-glycerol + phosphate
C6EFV6;
highest activity
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?
1-oleoyl-2-lyso-sn-glycero-3-phosphate + H2O
1-oleoyl-2-lyso-sn-glycerol + phosphate
C6EFV6;
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?
1-oleoyl-2-lyso-sn-glycero-3-phosphate + H2O
1-oleoyl-2-lyso-sn-glycerol + phosphate
C6EFV6;
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?
phosphatidylglycerol 3-phosphate + H2O
phosphatidylglycerol + phosphate
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?
phosphatidylglycerol 3-phosphate + H2O
phosphatidylglycerol + phosphate
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?
phosphatidylglycerol 3-phosphate + H2O
phosphatidylglycerol + phosphate
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?
phosphatidylglycerophosphate + H2O
?
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biosynthesis of phospholipids
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phosphatidylglycerophosphate + H2O
?
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phosphatidylglycerophosphate + H2O
?
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biosynthesis of phospholipids
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phosphatidylglycerophosphate + H2O
?
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biosynthesis of phospholipids
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phosphatidylglycerophosphate + H2O
?
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biosynthesis of phospholipids
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phosphatidylglycerophosphate + H2O
?
Micrococcus cerificans
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biosynthesis of phospholipids
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phosphatidylglycerophosphate + H2O
?
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phosphatidylglycerophosphate + H2O
?
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biosynthesis of phospholipids
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phosphatidylglycerophosphate + H2O
?
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phosphatidylglycerophosphate + H2O
?
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biosynthesis of phospholipids
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phosphatidylglycerophosphate + H2O
?
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biosynthesis of phospholipids
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phosphatidylglycerophosphate + H2O
?
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biosynthesis of phospholipids
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phosphatidylglycerophosphate + H2O
?
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biosynthesis of phospholipids
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phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
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?
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
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?
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
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?
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
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?
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
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hydrolysis of other simple phosphomonoesters not catalyzed
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phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
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?
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
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r
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
Micrococcus cerificans
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?
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
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phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
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?
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
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?
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
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?
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
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?
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
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?
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
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?
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
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r
undecaprenyl diphosphate + H2O
?
C6EFV6;
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?
undecaprenyl diphosphate + H2O
?
C6EFV6;
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?
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phosphatidylglycerophosphate + H2O
?
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
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?
undecaprenyl diphosphate + H2O
?
phosphatidylglycerophosphate + H2O
?
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biosynthesis of phospholipids
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phosphatidylglycerophosphate + H2O
?
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phosphatidylglycerophosphate + H2O
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biosynthesis of phospholipids
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phosphatidylglycerophosphate + H2O
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biosynthesis of phospholipids
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phosphatidylglycerophosphate + H2O
?
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biosynthesis of phospholipids
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phosphatidylglycerophosphate + H2O
?
Micrococcus cerificans
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biosynthesis of phospholipids
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phosphatidylglycerophosphate + H2O
?
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phosphatidylglycerophosphate + H2O
?
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biosynthesis of phospholipids
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phosphatidylglycerophosphate + H2O
?
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phosphatidylglycerophosphate + H2O
?
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biosynthesis of phospholipids
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phosphatidylglycerophosphate + H2O
?
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biosynthesis of phospholipids
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phosphatidylglycerophosphate + H2O
?
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biosynthesis of phospholipids
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phosphatidylglycerophosphate + H2O
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biosynthesis of phospholipids
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undecaprenyl diphosphate + H2O
?
C6EFV6
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?
undecaprenyl diphosphate + H2O
?
C6EFV6
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?
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Ca2+
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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
Mg2+
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addition of high concentrated divalent cations not required
Mg2+
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4 mM, not required for PGPB-tase
Mg2+
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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
Mg2+
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highest activity with 1 mM
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EDTA
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higher concentrations
ionic and non-ionic detergents
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most effective is Triton X-100
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octyl-beta-D-glucopyranoside
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complete inhibition with 30 mM
oleic acid
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higher than 1.5 mM
p-Chloromercuriphenylsulfonic acid
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100% inhibition at 1 mM
p-mercuribenzoic acid
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phosphatidic acid ammonium salt
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3.0 mM
phosphatidylglycerophosphate
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more than 100 æM
Sulfhydryl inhibitors
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trimethyloctadecyl ammonium chloride
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Ca2+
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Co2+
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Hg2+
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Hg2+
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complete inhibition at 1 mM
Hg2+
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complete inhibition at 0.5 mM
Mn2+
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NaF
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80% loss of activity with 5 mM in compound fraction of PGP-A, PGP-B and PGP-C
NaF
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70% inhibition at 1 mM
phosphate
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phosphate
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little effect up to 10 mM
Triton X-100
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high concentration
Triton X-100
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only in heat treatment
Zn2+
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oleic acid
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1.9 fold stimulation at 0.5 mM
phosphatidic acid sodium salt
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2 fold stimulation at 3.0 mM
EDTA
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1 mM
EDTA
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distinctly stimulatory at 1 mM
Triton X-100
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Triton X-100
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optimal at 1-1.5 mg/ml
Triton X-100
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up to 5 mM
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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
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0.002 - 0.18
phosphatidylglycerophosphate
0.002
phosphatidylglycerophosphate
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0.015
phosphatidylglycerophosphate
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0.08
phosphatidylglycerophosphate
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0.083
phosphatidylglycerophosphate
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0.18
phosphatidylglycerophosphate
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24
1,2-dioleoyl-sn-glycero-3-phosphate
C6EFV6;
pH and temperature not specified in the publication
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0.0017
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partially purified
0.0018
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pgpB geneproduct
0.0021
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pgpA geneproduct
0.0023
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partially purified
0.014
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compound of PGP-A,-B and -C
0.028
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partially purified
6
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PGPA-tase, more specific for phosphatidylglycerolphosphate than PGPB-tase
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7 - 8
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little activity below pH 7.0 and above pH 8.0
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C6EFV6;
trans-membrane protein
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trans-membrane protein
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weak association to the mitochondrial membrane
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Bacillus subtilis (strain 168);
A0A140N9T3
Escherichia coli (strain B / BL21-DE3);
P0A924
Escherichia coli (strain K12);
Neisseria meningitidis serogroup B (strain MC58);
O34349
Bacillus subtilis (strain 168);
O34349
Bacillus subtilis (strain 168);
Q66GT5
Mus musculus;
Q7DD94
Neisseria meningitidis serogroup B (strain MC58);
Q7DD94
Neisseria meningitidis serogroup B (strain MC58);
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29000
C6EFV6;
x * 29000, SDS-PAGE
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homotetramer
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x-ray crystallography
?
C6EFV6;
x * 29000, SDS-PAGE
?
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x * 29000, SDS-PAGE
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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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7.4
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95% activity for several weeks, stored in liquid nitrogen
94818
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43
C6EFV6;
the melting temperature of the wild type enzyme is 43°C
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50% loss of activity after solubilization with Triton X-100 in 12 h
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inactivation above 60°C
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PGP-C more sensitive to increasing temperature
presence of dithiothreitol required
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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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heat labile
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PGP-C more sensitive to increasing temperature
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PGP-C more sensitive to increasing temperature
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sensitive to sulfhydryl reagents and freeze-thaw cycles
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sensitive to sulfhydryl reagents and freeze-thaw cycles
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-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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GST-bind resin column chromatography
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purified in a detergent combination of nonyl-beta-D-glucopyranoside and n-dodecyl-N,N-dimethylamine-N-oxide
C6EFV6;
partial
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Escherichia coli strains lacking the original pgpA and/or pgpB genes
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expressed in Escherichia coli
C6EFV6;
expressed in Escherichia coli BL21 (DE3) cells
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expressed in Escherichia coli BL21 (DE3) CodonPlus RIPL cells
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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
-
the mutant shows strongly reduced activity
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H207A
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the mutant shows strongly reduced activity
-
K97A
-
the mutant shows strongly reduced activity
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R104A
-
the mutant shows strongly reduced activity
-
R201A
-
the mutant shows strongly reduced activity
-
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synthesis
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preparation of phosphatidylglycerophosphate
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Dutt, A.; Dowhan, W.
Intracellular distribution of enzymes of phospholipid metabolism in several gram-negative bacteria
J. Bacteriol.
132
159-165
1977
Escherichia coli, Klebsiella aerogenes, Micrococcus cerificans, Salmonella enterica subsp. enterica serovar Typhimurium, Serratia marcescens
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Cain, B.D.; Donohue, T.J.; Shepherd, W.D.; Kaplan, S.
Localization of phospholipid biosynthetic enzyme activities in cell-free fractions derived from Rhodopseudomonas sphaeroides
J. Biol. Chem.
259
942-948
1984
Escherichia coli
brenda
Griebau, R.; Frentzen , M.
Biosynthesis of phosphatidylglycerol in isolated mitochondria of etiolated mung bean (Vigna radiata) seedlings
Plant Physiol.
105
1269-1274
1994
Vigna radiata
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Cao, S.G.; Hatch, G.M.
Stimulation of phosphatidylglycerophosphate phosphatase activity by unsaturated fatty acids in rat heart
Lipids
29
475-480
1994
Rattus sp.
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Dowhan, W.; Funk, C.R.
Phosphatidylglycerophosphate phosphatase from Escherichia coli
Methods Enzymol.
209
224-230
1992
Escherichia coli
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Funk, C.R.; Zimniak, L.; Dowhan, W.
The pgpA and pgpB genes of Escherichia coli are not essential: evidence for a third phosphatidylglycerophosphate phosphatase
J. Bacteriol.
174
205-213
1992
Escherichia coli
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Kelly, B.L.; Greenberg, M.L.
Characterization and regulation of phosphatidylglycerophosphate phosphatase in Saccharomyces cerevisiae
Biochim. Biophys. Acta
1046
144-150
1990
Saccharomyces cerevisiae
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Chiu, T.; Yeh, L.L.
An improved preparation of phosphatidylglycerophosphate
Biochim. Biophys. Acta
876
167-169
1986
Streptococcus sanguinis
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Icho, T.; Raetz, C.R.H.
Multiple genes for membrane-bound phosphatases in Escherichia coli and their action on phospholipid precursors
J. Bacteriol.
153
722-730
1983
Rattus sp.
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Lipton, J.H.; McMurray, W.C.
Phosphatidyl glycerol phosphate phosphatase in BHK-21 cells. A comparison with rat liver mitochondria
Biochem. Biophys. Res. Commun.
73
300-305
1976
Mesocricetus auratus, Rattus sp.
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Larson, T.J.; Hirabayashi, T.; Dowhan, W.
Phosphatidylglycerol biosynthesis in Bacillus licheniformis. Resolution of membrane-bound enzymes by affinity chromatography on cytidinediphospho-sn-1,2-diacylglycerol sepharose
Biochemistry
15
974-979
1976
Bacillus licheniformis
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Chang, Y.; Kennedy, E.P.
Phosphatidyl glycerophosphate phosphatase
J. Lipid Res.
8
456-462
1967
Escherichia coli
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Wu, F.; Yang, Z.; Kuang, T.
Impaired photosynthesis in phosphatidylglycerol-deficient mutant of cyanobacterium Anabaena sp. PCC7120 with a disrupted gene encoding a putative phosphatidylglycerophosphatase
Plant Physiol.
141
1274-1283
2006
Anabaena sp., Anabaena sp. PCC 7120
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Kumaran, D.; Bonanno, J.B.; Burley, S.K.; Swaminathan, S.
Crystal structure of phosphatidylglycerophosphatase (PGPase), a putative membrane-bound lipid phosphatase, reveals a novel binuclear metal binding site and two 'proton wires'
Proteins
64
851-862
2006
Listeria monocytogenes
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Teh, P.G.; Chen, M.J.; Engel, J.L.; Worby, C.A.; Manning, G.; Dixon, J.E.; Zhang, J.
Identification of a mammalian-type phosphatidylglycerophosphate phosphatase in the Eubacterium Rhodopirellula baltica
J. Biol. Chem.
288
5176-5185
2013
Rhodopirellula baltica
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Fan, J.; Jiang, D.; Zhao, Y.; Liu, J.; Zhang, X.C.
Crystal structure of lipid phosphatase Escherichia coli phosphatidylglycerophosphate phosphatase B
Proc. Natl. Acad. Sci. USA
111
7636-7640
2014
Escherichia coli (C6EFV6), Escherichia coli, Escherichia coli B / ATCC 11303 (C6EFV6)
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