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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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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lipid metabolism
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Glycerophospholipid metabolism
-
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Metabolic pathways
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-
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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
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-
-
-
?
dipalmitoyl sn-glycero 3-phosphate + H2O
dipalmitoyl sn-glycerol + phosphate
show the reaction diagram
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-
-
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+
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-
EDTA
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higher concentrations
iodoacetamide
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ionic and non-ionic detergents
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most effective is Triton X-100
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Mg2+
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N-ethylmaleimide
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Octadecylamine
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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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phosphate
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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Triton X-100
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
arachidonic acid
-
-
EGTA
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0.01 - 0.10 mM
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
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
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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
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compound of PGP-A,-B and -C
0.028
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partially purified
0.13
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PGP-B and -C
0.19
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PGP-A and -C
5.2
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PGPC-tase
6
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PGPA-tase, more specific for phosphatidylglycerolphosphate than PGPB-tase
10.1
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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
ORGANISM
UNIPROT
Escherichia coli (strain B / BL21-DE3)
Escherichia coli (strain K12)
Neisseria meningitidis serogroup B (strain MC58)
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
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heat labile
heat stable up to 50°C
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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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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Triton X-100
-
-
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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)