Information on EC 3.1.3.18 - phosphoglycolate phosphatase

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

EC NUMBER
COMMENTARY hide
3.1.3.18
-
RECOMMENDED NAME
GeneOntology No.
phosphoglycolate phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-Phosphoglycolate + H2O = glycolate + phosphate
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
additional information
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-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
photorespiration
-
-
degradation of pentoses
-
-
Glyoxylate and dicarboxylate metabolism
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
2-phosphoglycolate phosphohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9025-76-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
ecotype Columbia
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
PCC6803
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
additional information
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-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-Chloroethyl-phosphate + H2O
Chloroethanol + phosphate
show the reaction diagram
-
-
-
-
-
2-Hydroxyethyl-phosphate + H2O
Hydroxyethanol + phosphate
show the reaction diagram
-
-
-
-
-
2-Phosphoglycolate + H2O
Glycolate + phosphate
show the reaction diagram
D-fructose-1,6-bisphosphate + H2O
D-fructose-1-phosphate + phosphate
show the reaction diagram
-
-
?
D-ribulose-5-phosphate + H2O
D-ribulose + phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Ethyl-phosphate + H2O
Ethanol + phosphate
show the reaction diagram
glycerol 1-phosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
?
i-Propyl-phosphate + H2O
i-Propanol + phosphate
show the reaction diagram
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slowly
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-
-
L-Phospholactate + H2O
L-Lactate + phosphate
show the reaction diagram
-
-
-
-
-
Methyl-phosphate + H2O
Methanol + phosphate
show the reaction diagram
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-
-
-
-
n-Propyl-phosphate + H2O
n-Propanol + phosphate
show the reaction diagram
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weak
-
-
-
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
phosphoglycolate + H2O
glycolate + phosphate
show the reaction diagram
additional information
?
-
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
2-Phosphoglycolate + H2O
Glycolate + phosphate
show the reaction diagram
glycerol 1-phosphate + H2O
glycerol + phosphate
show the reaction diagram
P19881
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
show the reaction diagram
P19881
-
-
-
?
phosphoglycolate + H2O
glycolate + phosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cs+
-
activates
K+
-
needed for optimal activation, can be replaced by Li+, Na+, Rb+, Cs+, NH4+
KCl
activates at chloride ion concentration up to 50 mM
Li+
-
activates
Na+
-
activates
NH4+
-
activates
Rb+
-
activates
ZnCl2
-
slight activation up to 0.1 mM
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoate)
-
-
6-phospho-gluconate
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isoenzyme I, french bean
alpha-alanine
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isoenzyme II, french bean
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
cysteine
-
-
diisopropylfluorophosphate
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-
formate
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isoenzyme I, french bean
fructose-6-phosphate
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isoenzyme I and II, french bean
glutamate
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isoenzyme II, french bean
glutathione
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glycine
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isoenzyme II, french bean
glycolate
glyoxylate
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isoenzyme II, french bean
iodoacetate
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-
Iodosobenzoate
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-
KCl
total inhibition at chloride ion concentration of 600 mM
p-chloromercuribenzoate
-
-
p-mercuribenzoic acid
the inhibition is recovered by addition of dithiothreitol
Phosphoglycolate * Mg2+ complex
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-
serine
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isoenzyme I, french bean
ZnCl2
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20% inhibition at 0.2 mM, 50% inhibition at 0.5 mM
additional information
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inactivated by lipase EC 3.1.1.3
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.3
2-Chloroethyl-phosphate
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-
0.54
2-Hydroxyethyl-phosphate
-
-
0.029 - 0.21
2-Phosphoglycolate
0.17 - 0.5
Co2+
0.17 - 3.1
diphosphate
0.15
ethyl-phosphate
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-
0.21
methyl-phosphate
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-
0.015 - 0.45
Mg2+
0.17 - 3.1
p-nitrophenyl phosphate
0.026 - 2
Phosphoglycolate
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.031 - 292
2-Phosphoglycolate
0.58 - 6.08
diphosphate
0.58 - 4.8
p-nitrophenyl phosphate
8.26
Phosphoglycolate
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
ZnCl2
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.94
p-nitrophenyl phosphate
5.98
-
-
7.4
substrate glycerol 1-phosphate, presence of 5 mM Mg2+
12.9
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17.7
substrate glycerol 2-phosphate, presence of 5 mM Mg2+
19.82
phosphoglycolate; substrate phosphoglycolate
99
-
-
107.5
substrate phosphoglycolate, presence of 5 mM Mg2+
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 9
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-
5.6 - 8
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6 - 8.5
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Chlamydomonas
6 - 7
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6 - 6.3
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6.3 - 8
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6.7 - 6.9
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isoenzyme I, french bean
6.7 - 7
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isoenzyme II, french bean
additional information
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-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
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-
5 - 9.5
5.5 - 9
6 - 8
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Anacystis, 6: 50% of maximum activity, 8: 20% of maximum activity
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.1
isoelectric focusing
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Escherichia coli (strain K12)
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)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20700
-
4 * 20700, SDS-PAGE, identical or nearly identical, Nicotiana tabacum
27000
1 * 27000, SDS-PAGE
27390
-
calculated from amino acid sequence
31500
-
2 * 31500, SDS-PAGE, Zea mays
32000
2 * 32000, SDS-PAGE
35000
-
2 * 35000, SDS-PAGE, human
50000
-
SDS-PAGE, 2 main protein bands with molecular weights of 50000 and 100000, Pisum sativum
61500
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polyacrylamide gradient gel electrophoresis, Zea mays
72000
-
human, sedimentation coefficient
79000
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human, gel filtation
80500
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Ferguson plot analysis, Nicotiana tabacum
86300
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sedimentation velocity on sucrose density gradients, Nicotiana tabacum
92000
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gel filtration, Chlamydomonas reinhardtii
93000
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Ferguson plot analysis, spinach
100000
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SDS-PAGE, 2 main protein bands with molecular weights of 50000 and 100000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
1 * 27000, SDS-PAGE
tetramer
-
4 * 20700, SDS-PAGE, identical or nearly identical, Nicotiana tabacum
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant protein, selenomethionine-labelled protein, hanging-drop vapour-diffusion method at 18C, polyethylene glycol 3500 as a precipitant and zinc acetate as an additive, data-collection and processing statistics
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Chlamydomonas enzyme stable, Anacystis enzyme labile
Citrate and isocitrate stabilize
-
stable
zinc coordination promotes the enzyme to a stable conformation
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 4 weeks, no significant loss of activity
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-20C, stable at least 6 months
-80C, as an ammonium sulfate paste, few months, loss of activity
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4C, 5% glycerol, 0.5 M NaCl, no loss in activity after several months
4C, 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
gel filtration, SDS-PAGE
Ni-NTA agarose affinity chromatography
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partial
the recombinant enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3), pET-22b expression vector
expressed in Escherichia coli strain LMG194
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plasmid ligation into pBluescript SKII (pBSKII) vector, expression in Escherichia coli DH5a
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G260S
-
40% activity compared to the wild type enzyme
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Show AA Sequence (9816 entries)
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