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Information on EC 3.1.3.27 - phosphatidylglycerophosphatase
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3.1.3.27 phosphatidylglycerophosphataseSpecify your search results
Word Map
- 3.1.3.27
- phosphatidylglycerol
- cardiolipin
- phospholipid
- mitochondrion
-
self-renewal
-
phosphatidylglycerolphosphate
-
pten-like
-
dual-specificity
-
phosphatidic
- alexidine
- synthesis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
At3g58830, At5g56610, PGP phosphatase, PGP-A, PGP-B, PGP-C, PGP-tase, PGPA-tase, PGPase, PgpB, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PGP phosphatase
PGPase
PgpB
Pgpp1
phosphatidylglycero phosphate phosphatase
-
-
-
-
phosphatidylglycerophosphate phosphatase B
PTPMT1
YodM
PGP phosphatase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
phosphatidylglycerophosphate + H2O = phosphatidylglycerol + phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
phosphatidylglycerophosphate phosphohydrolase
-
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CAS REGISTRY NUMBER
COMMENTARY
9033-46-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + H2O
1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + phosphate
1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O
1,2-dihexadecanoyl-sn-glycerol + phosphate
1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O
1-(9Z-octadecenoyl)-sn-glycerol + phosphate
dipalmitoyl sn-glycero 3-phosphate + H2O
dipalmitoyl sn-glycerol + phosphate
-
-
-
r
phosphatidylglycerophosphate + H2O
3-phosphatidylglycerol + phosphate
-
-
-
?
(2S,3R,4E)-2-aminooctadec-4-ene-1,3-diol-1-phosphate + H2O
?
-
-
-
?
1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + H2O
1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + phosphate
-
-
-
?
1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + H2O
1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + phosphate
-
-
-
?
1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O
1,2-dihexadecanoyl-sn-glycerol + phosphate
-
-
-
?
1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O
1,2-dihexadecanoyl-sn-glycerol + phosphate
-
-
-
?
1,2-dioleoyl-sn-glycero-3-phosphate + H2O
1,2-dioleoyl-sn-glycerol + phosphate
C6EFV6
highest activity
-
-
?
1,2-dioleoyl-sn-glycero-3-phosphate + H2O
1,2-dioleoyl-sn-glycerol + phosphate
Escherichia coli B / ATCC 11303
C6EFV6
highest activity
-
-
?
1,2-dipalmitoyl-sn-glycero-3-[phospho-rac-(1'-(3'-phospho)glycerol)] + H2O
? + phosphate
-
-
-
?
1,2-dipalmitoyl-sn-glycero-3-[phospho-rac-(1'-(3'-phospho)glycerol)] + H2O
? + phosphate
-
-
-
?
1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O
1-(9Z-octadecenoyl)-sn-glycerol + phosphate
-
-
-
?
1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O
1-(9Z-octadecenoyl)-sn-glycerol + phosphate
-
-
-
?
1-hexanoyl-sn-glycero-3-phosphate + H2O
1-hexanoyl-sn-glycerol + phosphate
-
-
-
?
1-hexanoyl-sn-glycero-3-phosphate + H2O
1-hexanoyl-sn-glycerol + phosphate
-
-
-
?
1-oleoyl-2-lyso-sn-glycero-3-phosphate + H2O
1-oleoyl-2-lyso-sn-glycerol + phosphate
C6EFV6
-
-
-
?
1-oleoyl-2-lyso-sn-glycero-3-phosphate + H2O
1-oleoyl-2-lyso-sn-glycerol + phosphate
Escherichia coli B / ATCC 11303
C6EFV6
-
-
-
?
isopentenyldiphosphate + H2O
isopentenylphosphate + phosphate
-
-
-
?
isopentenyldiphosphate + H2O
isopentenylphosphate + phosphate
-
-
-
?
phosphatidylglycerol 3-phosphate + H2O
phosphatidylglycerol + phosphate
-
-
-
-
?
phosphatidylglycerol 3-phosphate + H2O
phosphatidylglycerol + phosphate
-
-
-
-
?
phosphatidylglycerol 3-phosphate + H2O
phosphatidylglycerol + phosphate
-
-
-
-
?
phosphatidylglycerophosphate + H2O
?
-
biosynthesis of phospholipids
-
-
-
phosphatidylglycerophosphate + H2O
?
-
biosynthesis of phospholipids
-
-
-
phosphatidylglycerophosphate + H2O
?
-
biosynthesis of phospholipids
-
-
-
phosphatidylglycerophosphate + H2O
?
-
biosynthesis of phospholipids
-
-
-
phosphatidylglycerophosphate + H2O
?
Micrococcus cerificans
-
biosynthesis of phospholipids
-
-
-
phosphatidylglycerophosphate + H2O
?
-
biosynthesis of phospholipids
-
-
-
phosphatidylglycerophosphate + H2O
?
-
biosynthesis of phospholipids
-
-
-
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
-
-
-
?
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
-
-
-
?
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
-
-
-
?
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
-
-
-
?
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
-
-
-
?
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
-
hydrolysis of other simple phosphomonoesters not catalyzed
-
-
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
-
-
-
?
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
-
-
-
r
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
Micrococcus cerificans
-
-
-
?
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
-
-
-
-
?
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
-
-
-
?
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
-
-
-
?
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
-
-
-
?
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
-
-
-
r
undecaprenyldiphosphate + H2O
undecaprenylphosphate + phosphate
-
-
-
?
undecaprenyldiphosphate + H2O
undecaprenylphosphate + phosphate
-
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phosphatidylglycerophosphate + H2O
phosphatidylglycerol + phosphate
-
-
-
-
?
phosphatidylglycerophosphate + H2O
?
-
biosynthesis of phospholipids
-
-
-
phosphatidylglycerophosphate + H2O
?
-
biosynthesis of phospholipids
-
-
-
phosphatidylglycerophosphate + H2O
?
-
biosynthesis of phospholipids
-
-
-
phosphatidylglycerophosphate + H2O
?
-
biosynthesis of phospholipids
-
-
-
phosphatidylglycerophosphate + H2O
?
Micrococcus cerificans
-
biosynthesis of phospholipids
-
-
-
phosphatidylglycerophosphate + H2O
?
-
biosynthesis of phospholipids
-
-
-
phosphatidylglycerophosphate + H2O
?
-
biosynthesis of phospholipids
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
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
Mg2+
Mg2+
-
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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NaF
-
80% loss of activity with 5 mM in compound fraction of PGP-A, PGP-B and PGP-C
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.3
1,2-dioleoyl-sn-glycero-3-phosphate
C6EFV6
pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
24
1,2-dioleoyl-sn-glycero-3-phosphate
C6EFV6
pH and temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
-
PGPA-tase, more specific for phosphatidylglycerolphosphate than PGPB-tase
54.7
substrate 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate), pH 7.4, 37°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
weak association to the mitochondrial membrane
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
phosphatidylglycerophosphate phosphatase essential for the biosynthesis of cardiolipin, an integral component of mitochondrial and bacterial membranes
physiological function
physiological function
mutant plants lacking phosphatidylglycerophosphate phosphatase activity contain reduced amounts of chlorophyll, but photosynthetic quantum yield remains unchanged. The absolute content of plastidial phosphatidylglycerol (34:4; total number of acyl carbons:number of double bonds) is reduced by about 1/3. Expression of Pgpp1 gene complements the defect of a yeast Gep4 mutant
physiological function
expression of Ptpmt1 gene complements the phenotype of a yeast PGPP mutant. A Pgpp1 Ptpmt1 Ptpmt2 mutant significantly enhances the root phenotype of the Pgpp1 mutant without further affecting the photosynthesis; expression of Ptpmt2 gene complements the phenotype of a yeast PGPP mutant. A Pgpp1 Ptpmt1 Ptpmt2 mutant significantly enhances the root phenotype of the Pgpp1 mutant without further affecting the photosynthesis; mutants defective in Pgpp1 display considerably shorter roots, due to defective order of columella cells in the root apices. A Pgpp1 Ptpmt1 Ptpmt2 mutant additionally lacking mitochondria-localized phosphatases significantly enhances the root phenotype of the Pgpp1 mutant without further affecting the photosynthesis
physiological function
enzyme is the principal phosphatidylglycerol phosphate phosphatase of Bacillus subtilis. Gene expression complements both undecaprenylphosphate and phosphatidylglycerol metabolisms in Escherichia coli mutant strains
physiological function
-
enzyme is the principal phosphatidylglycerol phosphate phosphatase of Bacillus subtilis. Gene expression complements both undecaprenylphosphate and phosphatidylglycerol metabolisms in Escherichia coli mutant strains
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Bacillus subtilis (strain 168)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 25725, calculated from sequence; xs * 37550, calculated from sequence
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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
structure at 2.25 A resolution, with phosphate analogue tungstate in the active site. The structure reveals two lipid chains in the active site vicinity
vapor diffusion method, the structure is determined at 3.2 A resolution
with precipitant containing 30% pentaerythritol ethoxylate, 50 mM ammonium sulfate, 50 mM Bis-Tris at pH 6.5
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K93A
no significant change in activity with 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate), more than 50% increase in activity for undecaprenyldiphosphate and farnesyldiphosphate
K93A
-
no significant change in activity with 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate), more than 50% increase in activity for undecaprenyldiphosphate and farnesyldiphosphate
-
H163A
K93A
the mutant enzyme shows complete activity loss for lysophosphatidic acid and (2S,3R,4E)-2-aminooctadec-4-ene-1,3-diol-1-phosphate, whereas it retains full activity for phosphatidic acid and gains 40% more activity toward phosphatidylglycerol phosphate compared with wild type enzyme
K93A/K97A
the mutant enzyme shows complete activity loss for lysophosphatidic acid and (2S,3R,4E)-2-aminooctadec-4-ene-1,3-diol-1-phosphate, whereas it retains full activity for phosphatidic acid and gained 40% more activity toward phosphatidylglycerol phosphate compared with wild type enzyme
K93T
mutant enzyme with significantly improved activity for lysophosphatidic acid, (2S,3R,4E)-2-aminooctadec-4-ene-1,3-diol-1-phosphate, and phosphatidic acid by 2.5- or 3.4-fold but not for 1,2-dipalmitoryl-sn-glycero-3-[phospho-rac-(1'-(3'-phospho)glycerol)]
K93T/K97A
the mutant enzyme loses all activity for lysophosphatidic acid or (2S,3R,4E)-2-aminooctadec-4-ene-1,3-diol-1-phosphate, but retains 50% activity for phosphatidic acid or 1,2-dipalmitoryl-sn-glycero-3-[phospho-rac-(1'-(3'-phospho)glycerol)]
K97A
H163A
-
mutation increases hydrolysis of 1,2-dipalmitoryl-sn-glycero-3-[phospho-rac-(1'-(3'-phospho)glycerol)] by 50%
-
K93A
-
the mutant enzyme shows complete activity loss for lysophosphatidic acid and (2S,3R,4E)-2-aminooctadec-4-ene-1,3-diol-1-phosphate, whereas it retains full activity for phosphatidic acid and gains 40% more activity toward phosphatidylglycerol phosphate compared with wild type enzyme
-
K93A/K97A
-
the mutant enzyme shows complete activity loss for lysophosphatidic acid and (2S,3R,4E)-2-aminooctadec-4-ene-1,3-diol-1-phosphate, whereas it retains full activity for phosphatidic acid and gained 40% more activity toward phosphatidylglycerol phosphate compared with wild type enzyme
-
K97A
-
the mutant enzyme shows complete activity loss for lysophosphatidic acid and (2S,3R,4E)-2-aminooctadec-4-ene-1,3-diol-1-phosphate, whereas it retains full activity for phosphatidic acid and gained 40% more activity toward phosphatidylglycerol phosphate compared with wild type enzyme
-
H163A
mutation increases hydrolysis of 1,2-dipalmitoryl-sn-glycero-3-[phospho-rac-(1'-(3'-phospho)glycerol)] by 50%
K97A
the mutant enzyme shows complete activity loss for lysophosphatidic acid and (2S,3R,4E)-2-aminooctadec-4-ene-1,3-diol-1-phosphate, whereas it retains full activity for phosphatidic acid and gained 40% more activity toward phosphatidylglycerol phosphate compared with wild type enzyme
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
heat labile
PGP-C more sensitive to increasing temperature
sensitive to sulfhydryl reagents and freeze-thaw cycles
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, for weeks in 2% Triton X-100, 50 mM MgCl2, 20% glycerol, 0.5 M KCl
-
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
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
pgpB gene is cloned into the pET22b vector (Novagen) to generate the C-terminal His6-tagged protein. Mutants were generated using standard site-directed mutagenesis. The PgpB wild type and mutant proteins are expressed in Escherichia coli strain C41(DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
brenda
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
brenda
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.
brenda
Dowhan, W.; Funk, C.R.
Phosphatidylglycerophosphate phosphatase from Escherichia coli
Methods Enzymol.
209
224-230
1992
Escherichia coli
brenda
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
brenda
Kelly, B.L.; Greenberg, M.L.
Characterization and regulation of phosphatidylglycerophosphate phosphatase in Saccharomyces cerevisiae
Biochim. Biophys. Acta
1046
144-150
1990
Saccharomyces cerevisiae
brenda
Chiu, T.; Yeh, L.L.
An improved preparation of phosphatidylglycerophosphate
Biochim. Biophys. Acta
876
167-169
1986
Streptococcus sanguinis
brenda
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.
brenda
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.
brenda
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
brenda
Chang, Y.; Kennedy, E.P.
Phosphatidyl glycerophosphate phosphatase
J. Lipid Res.
8
456-462
1967
Escherichia coli
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
Zhou, Y.; Hölzl, G.; vom Dorp, K.; Peisker, H.; Melzer, M.; Frentzen, M.; Dörmann, P.
Identification and characterization of a plastidial phosphatidylglycerophosphate phosphatase in Arabidopsis thaliana
Plant J.
89
221-234
2017
Arabidopsis thaliana, Arabidopsis thaliana (Q84VV0)
brenda
Lin, Y.C.; Kobayashi, K.; Wada, H.; Nakamura, Y.
Phosphatidylglycerophosphate phosphatase is required for root growth in Arabidopsis
Biochim. Biophys. Acta
1863
563-575
2018
Arabidopsis thaliana, Arabidopsis thaliana (Q6NKR2), Arabidopsis thaliana (Q9ZQP1)
brenda
Ghachi, M.E.; Howe, N.; Auger, R.; Lambion, A.; Guiseppi, A.; Delbrassine, F.; Manat, G.; Roure, S.; Peslier, S.; Sauvage, E.; Vogeley, L.; Rengifo-Gonzalez, J.C.; Charlier, P.; Mengin-Lecreulx, D.; Foglino, M.; Touze, T.; Caffrey, M.; Kerff, F.
Crystal structure and biochemical characterization of the transmembrane PAP2 type phosphatidylglycerol phosphate phosphatase from Bacillus subtilis
Cell. Mol. Life Sci.
74
2319-2332
2017
Bacillus subtilis 168 (O34349), Bacillus subtilis (O34349)
brenda
Tong, S.; Lin, Y.; Lu, S.; Wang, M.; Bogdanov, M.; Zheng, L.
Structural insight into substrate selection and catalysis of lipid phosphate phosphatase PgpB in the cell membrane
J. Biol. Chem.
291
18342-18352
2016
Escherichia coli (P0A924), Escherichia coli K12 (P0A924)
brenda
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