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Information on EC 3.1.3.18 - phosphoglycolate phosphatase
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3.1.3.18 phosphoglycolate phosphataseSpecify your search results
The enzyme appears in viruses and cellular organisms
Synonyms
phosphoglycolate phosphatase, pgpase, 2-phosphoglycolate phosphatase, p-glycolate phosphatase, pglp1, slr0458, pglp2, sfpgpase, pho15, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-Phosphoglycolate phosphatase
Pgp
PGPase
Pho15
Phosphoglycolate phosphatase
photorespiratory enzyme
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-Phosphoglycolate + H2O = glycolate + phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
2-phosphoglycolate phosphohydrolase
-
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CAS REGISTRY NUMBER
COMMENTARY
9025-76-7
-
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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
1,3-dihydroxyacetone phosphate + H2O
1,3-dihydroxyacetone + phosphate
-
about 20% of the activity with 2-phosphoglycolate
-
?
2-glycerol phosphate + H2O
glycerol + phosphate
-
about 17% of the activity with 2-phosphoglycolate
-
?
D-fructose-1,6-bisphosphate + H2O
D-fructose-1-phosphate + phosphate
-
-
?
D-ribulose-5-phosphate + H2O
D-ribulose + phosphate
-
-
?
glyceraldehyde-3-phosphate + H2O
glyceraldehyde + phosphate
-
about 20% of the activity with 2-phosphoglycolate
-
?
2-Phosphoglycolate + H2O
Glycolate + phosphate
a key enzyme of photorespiration in photosynthetic organisms
-
?
2-Phosphoglycolate + H2O
Glycolate + phosphate
the enzyme is involved in a reaction relevant for DNA repair
-
?
2-Phosphoglycolate + H2O
Glycolate + phosphate
-
-
-
?
2-Phosphoglycolate + H2O
Glycolate + phosphate
-
first unique step of oxidative photosynthetic carbon cycle
-
?
2-Phosphoglycolate + H2O
Glycolate + phosphate
-
first unique step of oxidative photosynthetic carbon cycle
-
?
2-Phosphoglycolate + H2O
Glycolate + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
?
additional information
?
-
-
no substrates: phosphopeptides, 4-nitrophenylsulfate
-
?
additional information
?
-
-
no substrates: phosphopeptides, 4-nitrophenylsulfate
-
?
additional information
?
-
not: 3-phosphoglycerate, D-ribose-5-phosphate, phosphoenolpyruvate, O-phospho-1-serine, p-nitrophenylphosphate
-
?
additional information
?
-
-
not: 3-phosphoglycerate, D-ribose-5-phosphate, phosphoenolpyruvate, O-phospho-1-serine, p-nitrophenylphosphate
-
?
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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
2-Phosphoglycolate + H2O
Glycolate + phosphate
a key enzyme of photorespiration in photosynthetic organisms
-
?
2-Phosphoglycolate + H2O
Glycolate + phosphate
the enzyme is involved in a reaction relevant for DNA repair
-
?
2-Phosphoglycolate + H2O
Glycolate + phosphate
-
first unique step of oxidative photosynthetic carbon cycle
-
-
?
2-Phosphoglycolate + H2O
Glycolate + phosphate
-
first unique step of oxidative photosynthetic carbon cycle
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cl-
Co2+
Mg2+
Mn2+
Ni2+
Zn2+
additional information
Cl-
the activity is 11fold increased, cooperative effect of Cl- and Mg2+
Co2+
-
cations tested, in decreasing order of efficiency: Mn2+, Co2+, Mg2+, Ni2+
Co2+
-
cations tested, in decreasing order of efficiency: Mn2+, Co2+, Mg2+, Ni2+
Co2+
-
Anacystis: no activation, Chlamydomonas: activation
Mg2+
-
cations tested, in decreasing order of efficiency: Mn2+, Co2+, Mg2+, Ni2+
Mg2+
-
cations tested, in decreasing order of efficiency: Mn2+, Co2+, Mg2+, Ni2+
Mn2+
-
cations tested, in decreasing order of efficiency: Mn2+, Co2+, Mg2+, Ni2+
Mn2+
-
cations tested, in decreasing order of efficiency: Mn2+, Co2+, Mg2+, Ni2+
Ni2+
-
cations tested, in decreasing order of efficiency: Mn2+, Co2+, Mg2+, Ni2+
Ni2+
-
cations tested, in decreasing order of efficiency: Mn2+, Co2+, Mg2+, Ni2+
Zn2+
-
Anacystis: no activation, Chlamydomonas: activation
additional information
-
divalent cation required
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CaCl2
the enzyme binds to Ca2+, the inhibition is recovered by addition of EGTA and MgCl2
Cl-
inhibits at high concentration, above 50 mM, competitive inhibition; total inhibition at chloride ion concentration of 600 mM
NaCl
-
1 M, shift in oligomeric state of the protein from dimer towards monomer
p-mercuribenzoic acid
the inhibition is recovered by addition of dithiothreitol
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cl-
the activity is 11fold increased, cooperative effect of Cl- and Mg2+
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Anemia
Phosphoglycolate phosphatase and 2,3-diphosphoglycerate in red cells of normal and anemic subjects.
Anemia, Aplastic
Phosphoglycolate phosphatase and 2,3-diphosphoglycerate in red cells of normal and anemic subjects.
Anemia, Hemolytic
Phosphoglycolate phosphatase and 2,3-diphosphoglycerate in red cells of normal and anemic subjects.
Leprosy
Production and characterization of peptide mimotopes of phenolic glycolipid-I of Mycobacterium leprae.
phosphoglycolate phosphatase deficiency
A Photorespiratory Mutant of Chlamydomonas reinhardtii.
Polycystic Kidney, Autosomal Dominant
A study of genetic linkage heterogeneity in adult polycystic kidney disease.
Polycystic Kidney, Autosomal Dominant
Mapping of the familial Mediterranean fever gene to chromosome 16.
Polycystic Kidney, Autosomal Dominant
Two genetic markers closely linked to adult polycystic kidney disease on chromosome 16.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.3
2-Phosphoglycolate
pH not specified in the publication, temperature not specified in the publication
additional information
additional information
-
-
-
additional information
additional information
-
Km increases at higher pH, above 7.5
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.13
2-Phosphoglycolate
pH not specified in the publication, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
19.82
additional information
additional information
Rickettsia-like endosymbiont in the cytoplasm of Amoeba harbours plasmid with open-reading frame for phosphoglycolate phosphatase (PGPase), enzyme homologous to that of Bacillus cereus, contribution of plasmid-encoded phosphoglycolate phosphatase to the establishment of bacterial symbiosis within the hostile environment of amoeba cytoplasm
additional information
-
glycolate production in freely suspended and in alginate-immobilized cells
additional information
catalytic mechanism, dimerization behaviour and influence of metal ions on enzyme activity, recombinant protein, crystallization indicates the presence of two molecules in the asymmetric unit, structure determination using the multiwavelength anomalous dispersion (MAD) method, indicates that enzyme bears an alpha-helical cap domain that differs from that of a previously reported orthologue
additional information
-
catalytic mechanism, dimerization behaviour and influence of metal ions on enzyme activity, recombinant protein, crystallization indicates the presence of two molecules in the asymmetric unit, structure determination using the multiwavelength anomalous dispersion (MAD) method, indicates that enzyme bears an alpha-helical cap domain that differs from that of a previously reported orthologue
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.3
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9.5
5.5 - 9
6 - 8
-
Anacystis, 6: 50% of maximum activity, 8: 20% of maximum activity
additional information
5.5 - 9
-
Chlamydomonas: 40% of maximum activity at pH 5.0 and pH 9.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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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
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
cysteine residues Cys35, Cys104 and Cys243 in the catalytic core domain of PGP mediate the reversible inhibition of PGP activity and the associated, redox-dependent conformational changes. Cys35 oxidation weakens van-der-Waals interactions with Thr67, a conserved catalytic residue required for substrate coordination. Cys104 and Cys243 form a redox-dependent disulfide bridge between the PGP catalytic core and cap domains. Cys297 in the PGP cap domain is essential for redox-dependent PGP oligomerization, and PGP oxidation/oligomerization occurs in response to stimulation of cells with EGF
physiological function
physiological function
compared with the wild-type, the double mutant 1sll1349/slr0458 shows a 60% decrease in specific growth rates in low CO2-conditions
physiological function
-
knockdown of 2-phosphoglycolate phosphatase PGLP leads to distinct signs of the photorespiratory phenotype only below 5% residual PGLP protein. These lines are stunted in growth, have strongly increased 2-phosphoglycolate content, exhibit accelerated leaf senescence, and accumulate high amounts of branched-chain and aromatic amino acids. The ribulose-1,5-bisphosphate regeneration is cumulativly impaired with increased photorespiratory pressure
physiological function
PGP depletion facilitates fatty acid flux through the intracellular triacylglycerol/fatty acid cycle, and phosphatidylinositol-4,5-bisphosphate is critical for the impact of PGP activity on EGF-induced signaling. Loss of endogenous PGP expression amplifies both EGF-induced EGF receptor autophosphorylation and Src-dependent tyrosine phosphorylation of phospholipase C-gamma1. EGF enhances the formation of circular dorsal ruffles in PGP-depleted cells via Src/PLCgamma1/protein kinase C (PKC)-dependent signaling to the cytoskeleton
physiological function
-
protein is essential for parasite survival during asexual stages
physiological function
replacement of murine Pgp with its phosphatase-inactive PgpD34N mutant is embryonically lethal due to intrauterine growth arrest and developmental delay in midgestation. PGP inactivation attenuates triosephosphate isomerase activity, increases triglyceride levels at the expense of the cellular phosphatidylcholine content, and inhibits cell proliferation. These effects are prevented under hypoxic conditions or by blocking phosphoglycolate release from damaged DNA
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Aquifex aeolicus (strain VF5)
Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081 / JCM 1002 / NBRC 13953 / NCIMB 11778)
Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
-
SDS-PAGE, 2 main protein bands with molecular weights of 50000 and 100000
20700
-
4 * 20700, SDS-PAGE, identical or nearly identical, Nicotiana tabacum
50000
-
SDS-PAGE, 2 main protein bands with molecular weights of 50000 and 100000, Pisum sativum
86300
-
sedimentation velocity on sucrose density gradients, Nicotiana tabacum
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
tetramer
-
4 * 20700, SDS-PAGE, identical or nearly identical, Nicotiana tabacum
additional information
additional information
SEC-multi angle light scattering analysis, the mass fractions show a tetramer/dimer distribution of 13.8/ 84.5% for untreated PGP, and of 6.6/92.5% for the tris(2-carboxyethyl)phosphine-treated enzyme
additional information
-
SEC-multi angle light scattering analysis, the mass fractions show a tetramer/dimer distribution of 13.8/ 84.5% for untreated PGP, and of 6.6/92.5% for the tris(2-carboxyethyl)phosphine-treated enzyme
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
protein-ligand interaction analysis. The Cys26 thiol group can engage in a van-der-Waals interaction with Ser58. The reduction-induced conformational change in wild-type is likely triggered by loss of the Cys104/Cys243 disulfide bridge between the PGP core and cap domains
recombinant protein, selenomethionine-labelled protein, hanging-drop vapour-diffusion method at 18°C, polyethylene glycol 3500 as a precipitant and zinc acetate as an additive, data-collection and processing statistics
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D34N
phosphatase-inactive mutant. Knockin replacement of murine Pgp with its D34N mutant is embryonically lethal
additional information
additional information
-
T-DNA knockout of PGLP1 or PGLP2 (mutant At5g36700) results in very low leaf PGLP activity
additional information
-
immobilization of the cells in alginate increases the photorespiration rate and the enzyme activity compared to freely suspended cells, overview
additional information
-
immobilization of the cells in alginate increases the photorespiration rate and the enzyme activity compared to freely suspended cells, overview
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Chlamydomonas enzyme stable, Anacystis enzyme labile
free phosphatase rapidly precipitates under all the conditions tested
stable
Chlamydomonas enzyme stable, Anacystis enzyme labile
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 5% glycerol, 0.5 M NaCl, no loss in activity after several months
4°C, 50 mM KCl, 2 mM MgCl2, 2.5 mg/ml bovine serum albumin, 3 weeks, 50% loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
plasmid ligation into pBluescript SKII (pBSKII) vector, expression in Escherichia coli DH5a
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Baldy, P.; Piquemal, M.; Cavalie, G.
Phosphoglycolate phosphatase: immunological comparisons of the enzyme from the different photosynthetic groups of plants using maize polyclonal antiserum
Plant Sci.
60
9-20
1989
Amaranthus caudatus, Glycine max, Hordeum vulgare, More, Megathyrsus maximus, Panicum miliaceum, Panicum milioides, Sorghum bicolor, Triticum aestivum, Zea mays
-
brenda
Huh, D.H.; Kursell, A.V.; Husic, H.D.
Kinetic properties of phosphoglycolate phosphatase from Pisum sativum and Phaseolus vulgaris
Phytochemistry
28
719-720
1989
Pisum sativum
-
brenda
Rose, Z.B.; Grove, D.S.; Seal, S.N.
Mechanism of activation by anions of phosphoglycolate phosphatases from spinach and human red blood cells
J. Biol. Chem.
261
10996-11002
1986
Homo sapiens, Spinacia oleracea
brenda
Hardy, P.; Baldy, P.
Corn phosphoglycolate phosphatase: purification and properties
Planta
168
245-252
1986
Zea mays
brenda
Husic, H.D.; Tolbert, N.E.
Properties of phosphoglycolate phosphatase from Chlamydomonas reinhardtii and Anacystis nidulans
Plant Physiol.
79
394-399
1985
Trichormus variabilis, Synechococcus elongatus PCC 7942 = FACHB-805, Chlamydomonas reinhardtii, Chlorella vulgaris
brenda
Husic, H.D.; Tolbert, N.E.
Anion and divalent cation activation of phosphoglycolate phosphatase from leaves
Arch. Biochem. Biophys.
229
64-72
1984
Spinacia oleracea
brenda
Rose, Z.B.
Phosphoglycolate phosphatase from human red blood cells
Arch. Biochem. Biophys.
208
602-609
1981
Homo sapiens
brenda
Zecher, R.; Wolf, H.U.
Partial purification and characterization of human erythrocyte phosphoglycollate phosphatase
Biochem. J.
191
117-124
1980
Homo sapiens
brenda
Verin-Vergeau, C.; Baldy, P.; Cavalie, G.
Phosphoglycolate phosphatases from French bean leaves: catalytic properties of two isoenzymes
Phytochemistry
19
763-767
1980
Phaseolus vulgaris
-
brenda
Verin-Vergeau, C.; Baldy, P.; Cavalie, G.
Phosphoglycolate phosphatase from haricot leaves: two isofunctional forms
Phytochemistry
18
1279-1282
1979
Phaseolus vulgaris
-
brenda
Badwey, J.A.
Phosphoglycolate phosphatase in human erythrocytes
J. Biol. Chem.
252
2441-2443
1977
Homo sapiens
brenda
Kerr, M.W.; Gear, C.F.
Phosphoglycolate phosphatase isolated from pea leaves
Biochem. Soc. Trans.
2
338-340
1974
Pisum sativum
-
brenda
Beutler, E.; West, C.
An improved assay and some properties of phosphoglycolate phosphatase
Anal. Biochem.
106
163-168
1980
Rattus norvegicus
brenda
Christeller, J.T.; Tolbert, N.E.
Phosphoglycolate phosphatase. Purification and properties
J. Biol. Chem.
253
1780-1785
1978
Nicotiana tabacum
brenda
Christeller, J.T.; Tolbert, N.E.
Mechanism of phosphoglycolate phosphatase. Studies of hydrolysis and transphosphorylation, substrate analogs, and sulfhydryl inhibition
J. Biol. Chem.
253
1791-1798
1978
Nicotiana tabacum
brenda
Christeller, J.T.; Tolbert, N.E.
Phosphoglycolate phosphatase. Effect of cation and pH on activity
J. Biol. Chem.
253
1786-1790
1978
Nicotiana tabacum
brenda
Richardson, K.E.; Tolbert, N.E.
Phosphoglycolic acid phosphatase
J. Biol. Chem.
236
1285-1290
1961
Nicotiana tabacum
brenda
Pellicer, M.T.; Nunez, M.F.; Aguilar, J.; Badia, J.; Baldoma, L.
Role of 2-phosphoglycolate phosphatase of Escherichia coli in metabolism of the 2-phosphoglycolate formed in DNA repair
J. Bacteriol.
185
5815-5821
2003
Agrobacterium tumefaciens, Cupriavidus necator, Escherichia coli, Escherichia coli (P32662), Salmonella enterica, Haemophilus influenzae, Shigella flexneri, Klebsiella aerogenes (Q9EYY5)
brenda
Mamedov, T.G.; Suzuki, K.; Miura, K.; Kucho Ki, K.; Fukuzawa, H.
Characteristics and sequence of phosphoglycolate phosphatase from a eukaryotic green alga Chlamydomonas reinhardtii
J. Biol. Chem.
276
45573-45579
2001
Triticum aestivum, Aquifex aeolicus (O67359), Escherichia coli (P32662), Cupriavidus necator (P40852), Synechocystis sp. (P73525), Chlamydomonas reinhardtii (Q948T5), Chlamydomonas reinhardtii
brenda
Kim, Y.; Yakunin, A.F.; Kuznetsova, E.; Xu, X.; Pennycooke, M.; Gu, J.; Cheung, F.; Proudfoot, M.; Arrowsmith, C.H.; Joachimiak, A.; Edwards, A.M.; Christendat, D.
Structure- and function-based characterization of a new phosphoglycolate phosphatase from Thermoplasma acidophilum
J. Biol. Chem.
279
517-526
2004
Homo sapiens, Spinacia oleracea, Thermoplasma acidophilum (Q9HLQ2), Thermoplasma acidophilum
brenda
Garbayo, I.; Forja, E.; Salguero, A.; Cuaresma, M.; Vegaz, J.M.; Ichez, C.V.
Enhancement of photorespiration in immobilized Chlamydomonas reinhardtii cells
Biotechnol. Lett.
27
265-267
2005
Chlamydomonas reinhardtii, Chlamydomonas reinhardtii 21
brenda
Proudfoot, M.
corresponding Author: Dr. Alexander Yakunin, C.H. Best Institute, 112 College St. Room 72, Toronto On M5G 1L6, Canada
Private Communication
10
1-1
2007
Saccharomyces cerevisiae (P19881)
-
brenda
Schwarte, S.; Bauwe, H.
Identification of the photorespiratory 2-phosphoglycolate phosphatase, PGLP1, in Arabidopsis
Plant Physiol.
144
1580-1586
2007
Arabidopsis thaliana
brenda
Liu, H.; Zhou, H.; Zhu, D.; Bi, R.
Overexpression, purification, characterization and preliminary crystallographic study of phosphoglycolate phosphatase from Shigella flexneri 2a strain 301
Acta Crystallogr. Sect. F
F65
29-33
2009
Shigella flexneri (Q83PX1), Shigella flexneri
brenda
Park, M.; Kim, M.S.; Lee, K.M.; Hwang, S.Y.; Ahn, T.I.
Characterization of a cryptic plasmid from an alpha-proteobacterial endosymbiont of Amoeba proteus
Plasmid
61
78-87
2009
alpha proteobacterium endosymbiont of Amoeba proteus (B3VBH3)
brenda
Segerer, G.; Engelmann, D.; Kaestner, A.; Troetzmueller, M.; Koefeler, H.; Stigloher, C.; Thiele, C.; Jeanclos, E.; Gohla, A.
A phosphoglycolate phosphatase/AUM-dependent link between triacylglycerol turnover and epidermal growth factor signaling
Biochim. Biophys. Acta
1863
584-594
2018
Mus musculus (Q8CHP8)
brenda
Krocova, E.; Neradova, S.; Kupcik, R.; Janovska, S.; Bilkova, Z.; Heidingsfeld, O.
PHO15 genes of Candida albicans and Candida parapsilosis encode HAD-type phosphatases dephosphorylating 2-phosphoglycolate
FEMS Yeast Res.
19
foy112
2019
Candida albicans, Candida parapsilosis
brenda
Seifried, A.; Bergeron, A.; Boivin, B.; Gohla, A.
Reversible oxidation controls the activity and oligomeric state of the mammalian phosphoglycolate phosphatase AUM
Free Radic. Biol. Med.
97
75-84
2016
Mus musculus (Q8CHP8), Mus musculus
brenda
Rai, S.; Lucius, S.; Kern, R.; Bauwe, H.; Kaplan, A.; Kopka, J.; Hagemann, M.
The Synechocystis sp. PCC 6803 genome encodes up to four 2-phosphoglycolate phosphatases
Front. Plant Sci.
9
1718
2018
Synechocystis sp. PCC 6803 (P74697)
brenda
Nagappa, L.K.; Satha, P.; Govindaraju, T.; Balaram, H.
Phosphoglycolate phosphatase is a metabolic proof-reading enzyme essential for cellular function in Plasmodium berghei
J. Biol. Chem.
294
4997-5007
2019
Plasmodium berghei
brenda
Levey, M.; Timm, S.; Mettler-Altmann, T.; Luca Borghi, G.; Koczor, M.; Arrivault, S.; Pm Weber, A.; Bauwe, H.; Gowik, U.; Westhoff, P.
Efficient 2-phosphoglycolate degradation is required to maintain carbon assimilation and allocation in the C4 plant Flaveria bidentis
J. Exp. Bot.
70
575-587
2019
Flaveria bidentis
brenda
Segerer, G.; Hadamek, K.; Zundler, M.; Fekete, A.; Seifried, A.; Mueller, M.J.; Koentgen, F.; Gessler, M.; Jeanclos, E.; Gohla, A.
An essential developmental function for murine phosphoglycolate phosphatase in safeguarding cell proliferation
Sci. Rep.
6
35160
2016
Mus musculus (Q8CHP8), Mus musculus
brenda
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