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Literature summary for 3.1.4.38 extracted from

  • Sugimori, D.; Ogasawara, J.; Okuda, K.; Murayama, K.
    Purification, characterization, molecular cloning, and extracellular production of a novel bacterial glycerophosphocholine cholinephosphodiesterase from Streptomyces sanglieri (2014), J. Biosci. Bioeng., 117, 422-430.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
2-mercaptoethanol
-
Streptomyces sanglieri
EDTA 13% activation at 2 mM Streptomyces sanglieri
additional information poor activation by 2 mM DTT and SDS Streptomyces sanglieri

Cloned(Commentary)

Cloned (Comment) Organism
gene gpc-cp, DNA and amino acid sequence determination and analysis, sequence comparison and phyogenetic tree, peptide sequencing, molecular cloning in Escherichia coli strain HST08, recombinant expression of the C-terminally His6-tagged enzyme in enzyme-lacking Streptomyces lividans strain 1326 (NBRC15675) Streptomyces sanglieri

Inhibitors

Inhibitors Comment Organism Structure
Co2+ 80.6% inhibition at 2 mM Streptomyces sanglieri
Cu2+ complete inhibition at 2 mM Streptomyces sanglieri
Fe2+ 49.4% inhibition at 2 mM Streptomyces sanglieri
Mn2+ 20.5% inhibition at 2 mM Streptomyces sanglieri
additional information no inhibition by 2 mM SDS or DTT, poor inhibition by 2 mm iodoacetamide Streptomyces sanglieri
PMSF 21.2% inhibition at 2 mM Streptomyces sanglieri
Zn2+ 99.6% inhibition at 2 mM Streptomyces sanglieri

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.41
-
sn-glycerol-3-phosphocholine pH 7.2, 37°C Streptomyces sanglieri

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Streptomyces sanglieri
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ 14% activation at 2 mM Streptomyces sanglieri
additional information the enzyme is metal ion-independent, no effect by 2 mm Mg2+ and K+ Streptomyces sanglieri
Na+ 11% activation at 2 mM Streptomyces sanglieri

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
66000
-
native enzyme, gel filtration Streptomyces sanglieri
70447
-
1 * 66000, SDS-PAGE, 1 * 70447, sequence calculation Streptomyces sanglieri

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
sn-glycero-3-phosphocholine + H2O Streptomyces sanglieri
-
glycerol + phosphocholine
-
?
sn-glycero-3-phosphocholine + H2O Streptomyces sanglieri A14
-
glycerol + phosphocholine
-
?

Organism

Organism UniProt Comment Textmining
no activity in Streptomyces lividans
-
NBRC15675
-
no activity in Streptomyces lividans 1326
-
NBRC15675
-
Streptomyces sanglieri U6C6H1 isolation and identification, gene gpc-cp
-
Streptomyces sanglieri A14 U6C6H1 isolation and identification, gene gpc-cp
-

Purification (Commentary)

Purification (Comment) Organism
recombinant C-terminally His6-tagged enzyme from Streptomyces lividans strain 1326 by ammonium sulfate fractionation, nickel affinity and hydrophobic interaction chromatography, native extracellular enzyme 53fold from culture supernatant by ammonium sulfate fractionation, dialysis, anion exchange chromatography, and ultrafiltration, followed by hydrophobic interaction chromatography, ultrafiltration, two different steps of anion exxchange chromatography, ultrafiltration, gel filtration, ultrafiltration, cation exchange chromatography, and again ultrafiltration Streptomyces sanglieri

Source Tissue

Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
282
-
purified recombinant His-tagged enzyme, pH 7.2, 37°C Streptomyces sanglieri
583
-
purified native enzyme, pH 7.2, 37°C Streptomyces sanglieri

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-alpha-lysophosphatidylcholine + H2O
-
Streptomyces sanglieri ?
-
?
L-alpha-lysophosphatidylcholine + H2O
-
Streptomyces sanglieri A14 ?
-
?
additional information substrate specificity, overview. The enzyme exhibits specificity toward glycerol-3-phosphocholine and glycerol-3-phosphoethanolamine and hydrolyzes glycerol-3-phosphate and lysophosphatidylcholine. The enzyme shows no activity toward any diacylglycerophospholipids and little activity toward other glycerol-3-phosphodiesters and lysophospholipids, no activity with sn-glycerol-3-phosphoserine, L-alpha-lysophosphatidylinositol, L-alpha-lysophosphatidylserine, L-alpha-lysophosphatidylglycerol, 1,2-dipalmitoyl-sn-glycero-3-phosphocholine, 1,2-dimyristoyl-snglycero-3-phosphate, 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-rac-(1-glycerol), L-alpha-phosphatidylinositol, sphingomyelin, beta-acetyl-gamma-sn-hexadecyl-L-alpha-phosphatidylcholine, or 1-O-1'-(Z)-octadecenyl-2-hydroxy-sn-glycero-3-phosphoethanolamine, poor activity with 1-O-1'-(Z)-octadecenyl-2-hydroxy-sn-glycero-3-phosphocholine, L-alpha-lysophosphatidylethanolamine, or 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-L-serine Streptomyces sanglieri ?
-
?
additional information substrate specificity, overview. The enzyme exhibits specificity toward glycerol-3-phosphocholine and glycerol-3-phosphoethanolamine and hydrolyzes glycerol-3-phosphate and lysophosphatidylcholine. The enzyme shows no activity toward any diacylglycerophospholipids and little activity toward other glycerol-3-phosphodiesters and lysophospholipids, no activity with sn-glycerol-3-phosphoserine, L-alpha-lysophosphatidylinositol, L-alpha-lysophosphatidylserine, L-alpha-lysophosphatidylglycerol, 1,2-dipalmitoyl-sn-glycero-3-phosphocholine, 1,2-dimyristoyl-snglycero-3-phosphate, 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-rac-(1-glycerol), L-alpha-phosphatidylinositol, sphingomyelin, beta-acetyl-gamma-sn-hexadecyl-L-alpha-phosphatidylcholine, or 1-O-1'-(Z)-octadecenyl-2-hydroxy-sn-glycero-3-phosphoethanolamine, poor activity with 1-O-1'-(Z)-octadecenyl-2-hydroxy-sn-glycero-3-phosphocholine, L-alpha-lysophosphatidylethanolamine, or 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-L-serine Streptomyces sanglieri A14 ?
-
?
sn-glycero-3-phosphocholine + H2O
-
Streptomyces sanglieri glycerol + phosphocholine
-
?
sn-glycero-3-phosphocholine + H2O
-
Streptomyces sanglieri A14 glycerol + phosphocholine
-
?
sn-glycerol-3-phosphate + H2O lower activity Streptomyces sanglieri glycerol + phosphate
-
?
sn-glycerol-3-phosphate + H2O lower activity Streptomyces sanglieri A14 glycerol + phosphate
-
?
sn-glycerol-3-phosphocholine + H2O best substrate Streptomyces sanglieri glycerol + phosphocholine
-
?
sn-glycerol-3-phosphocholine + H2O best substrate Streptomyces sanglieri A14 glycerol + phosphocholine
-
?
sn-glycerol-3-phosphoethanolamine + H2O high activity Streptomyces sanglieri glycerol + phosphoethanolamine
-
?

Subunits

Subunits Comment Organism
monomer 1 * 66000, SDS-PAGE, 1 * 70447, sequence calculation Streptomyces sanglieri

Synonyms

Synonyms Comment Organism
GPC-CP
-
Streptomyces sanglieri
GPC-CP14
-
Streptomyces sanglieri

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
-
Streptomyces sanglieri

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
37 60 activity range with over 95% of maximal activity Streptomyces sanglieri

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4 45 completely stable at Streptomyces sanglieri
50
-
purified extracellular enzyme, 30 min, stable at Streptomyces sanglieri

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
29
-
sn-glycerol-3-phosphocholine pH 7.2, 37°C Streptomyces sanglieri

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
-
Streptomyces sanglieri

pH Range

pH Minimum pH Maximum Comment Organism
6 9 narrow pH range near pH 7 Streptomyces sanglieri

pH Stability

pH Stability pH Stability Maximum Comment Organism
5 10.5 purified extracellular enzyme, 30 min, stable at Streptomyces sanglieri

General Information

General Information Comment Organism
evolution the enzyme may be a member of the PLC/acid phosphatase protein superfamily, and the member of a distinct family, unlike glycerophosphocholine phosphodiesterase (EC 3.1.4.2) and alkaline phosphatase (EC 3.1.3.1) Streptomyces sanglieri
metabolism sn-glycerol-3-phosphocholine hydrolysis by the enzme might represent a different metabolic pathway for acquisition of a phosphorus source in actinomycetes Streptomyces sanglieri

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
20.6
-
sn-glycerol-3-phosphocholine pH 7.2, 37°C Streptomyces sanglieri