Information on EC 3.1.3.27 - phosphatidylglycerophosphatase

New: Word Map on EC 3.1.3.27
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY hide
3.1.3.27
-
RECOMMENDED NAME
GeneOntology No.
phosphatidylglycerophosphatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
phosphatidylglycerophosphate + H2O = phosphatidylglycerol + phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
cardiolipin biosynthesis
-
-
cardiolipin biosynthesis I
-
-
cardiolipin biosynthesis II
-
-
cardiolipin biosynthesis III
-
-
Glycerophospholipid metabolism
-
-
lipid metabolism
-
-
Metabolic pathways
-
-
phosphatidylglycerol biosynthesis I (plastidic)
-
-
phosphatidylglycerol biosynthesis II (non-plastidic)
-
-
SYSTEMATIC NAME
IUBMB Comments
phosphatidylglycerophosphate phosphohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9033-46-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain PCC7120
-
-
Manually annotated by BRENDA team
Anabaena sp. PCC7120
strain PCC7120
-
-
Manually annotated by BRENDA team
Syrian hamster
-
-
Manually annotated by BRENDA team
Micrococcus cerificans
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
bakers yeast
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
phosphatidylglycerophosphate phosphatase essential for the biosynthesis of cardiolipin, an integral component of mitochondrial and bacterial membranes
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
highest activity
-
-
?
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
-
-
-
?
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
C6EFV6
-
-
-
?
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
-
-
EDTA
-
higher concentrations
iodoacetamide
-
-
ionic and non-ionic detergents
-
most effective is Triton X-100
-
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
-
more than 100 M
Sulfhydryl inhibitors
-
-
-
trimethyloctadecyl ammonium chloride
-
-
Triton X-100
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3
1,2-dioleoyl-sn-glycero-3-phosphate
pH and temperature not specified in the publication
0.012
dipalmitoyl sn-glycero 3-phosphate
-
-
0.002 - 0.18
phosphatidylglycerophosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
24
1,2-dioleoyl-sn-glycero-3-phosphate
Escherichia coli
C6EFV6
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0004
-
-
0.0017
-
partially purified
0.0018
-
pgpB geneproduct
0.0021
-
pgpA geneproduct
0.0023
-
partially purified
0.01
-
PGP-C
0.014
-
compound of PGP-A,-B and -C
0.028
-
partially purified
0.13
-
PGP-B and -C
0.19
-
PGP-A and -C
5.2
-
PGPC-tase
6
-
PGPA-tase, more specific for phosphatidylglycerolphosphate than PGPB-tase
10.1
-
PGPB-tase
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
-
little activity below pH 7.0 and above pH 8.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain B / BL21-DE3)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 29000, SDS-PAGE
homotetramer
-
x-ray crystallography
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
vapor diffusion method
with precipitant containing 30% pentaerythritol ethoxylate, 50 mM ammonium sulfate, 50 mM Bis-Tris at pH 6.5
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
95% activity for several weeks, stored in liquid nitrogen
94818
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43
the melting temperature of the wild type enzyme is 43C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
50% loss of activity after solubilization with Triton X-100 in 12 h
-
heat labile
heat stable up to 50C
-
inactivation above 60C
-
PGP-C more sensitive to increasing temperature
presence of dithiothreitol required
-
resistant to solubilization with Triton X-100 if 5 mM EDTA is included
-
sensitive to sulfhydryl reagents and freeze-thaw cycles
the enzyme is stabilized by Na2MoO4 but not by Na2SO4
unstable at room temperature
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Triton X-100
-
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable for several months in 0.25 sucrose, 0.1 mM EDTA, pH 7.4
-
-20C, stable for weeks
-
4C, for weeks in 2% Triton X-100, 50 mM MgCl2, 20% glycerol, 0.5 M KCl
-
4C, 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
-
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
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Escherichia coli strains lacking the original pgpA and/or pgpB genes
-
expressed in Escherichia coli
expressed in Escherichia coli BL21 (DE3) cells
-
expressed in Escherichia coli BL21 (DE3) CodonPlus RIPL cells
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A83F
the mutant shows reduced activity
D211E
the mutant shows strongly reduced activity
F61W
the mutant shows reduced activity
G89L
the mutant shows strongly reduced activity
G91M
the mutant shows reduced activity
H163A
the mutant shows strongly reduced activity
H207A
the mutant shows strongly reduced activity
H57F
the mutant shows about wild type activity
K93E
the mutant shows reduced activity
K97A
the mutant shows strongly reduced activity
L58F
the mutant shows about wild type activity
Q90A
the mutant shows reduced activity
R104A
the mutant shows strongly reduced activity
R201A
the mutant shows strongly reduced activity
V54F
the mutant shows reduced activity
V88F
the mutant shows reduced activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
-
preparation of phosphatidylglycerophosphate
Show AA Sequence (4214 entries)
Please use the Sequence Search for a certain query.