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Literature summary extracted from

  • Sugimori, D.; Kano, K.; Matsumoto, Y.
    Purification, characterization, molecular cloning and extracellular production of a phospholipase A1 from Streptomyces albidoflavus NA297 (2012), FEBS open bio, 2, 318-327.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.32 gene pla, DNA and amino acid sequence determination and analysis, expression and extracellular production of the recombinant enzyme in Streptomyces lividans from expression vector pUC702/pla Streptomyces albidoflavus

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.32 H218A site-directed mutagenesis, inactive mutant Streptomyces albidoflavus
3.1.1.32 H218R site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Streptomyces albidoflavus
3.1.1.32 S11A site-directed mutagenesis, inactive mutant Streptomyces albidoflavus
3.1.1.32 S11D site-directed mutagenesis, inactive mutant Streptomyces albidoflavus
3.1.1.32 S11E site-directed mutagenesis, inactive mutant Streptomyces albidoflavus
3.1.1.32 S11T site-directed mutagenesis, inactive mutant Streptomyces albidoflavus
3.1.1.32 S11Y site-directed mutagenesis, inactive mutant Streptomyces albidoflavus
3.1.1.32 S216A site-directed mutagenesis, inactive mutant Streptomyces albidoflavus
3.1.1.32 S216D site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Streptomyces albidoflavus
3.1.1.32 S216E site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Streptomyces albidoflavus
3.1.1.32 S216T site-directed mutagenesis, the mutant shows 80-90% reduced activity compared to the wild-type enzyme Streptomyces albidoflavus
3.1.1.32 S216Y site-directed mutagenesis, the mutant shows 80-90% reduced activity compared to the wild-type enzyme Streptomyces albidoflavus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.32 2-mercaptoethanol weak inhibition Streptomyces albidoflavus
3.1.1.32 Ca2+ up to 0.1 mM Streptomyces albidoflavus
3.1.1.32 Fe2+
-
 Streptomyces albidoflavus
3.1.1.32 Fe3+
-
 Streptomyces albidoflavus
3.1.1.32 additional information the enzyme is not inhibited by EDTA and DTT Streptomyces albidoflavus
3.1.1.32 PMSF weak inhibition Streptomyces albidoflavus
3.1.1.32 SDS
-
 Streptomyces albidoflavus
3.1.1.32 Triton X-100 weak inhibition at up to 0.23% w/v Streptomyces albidoflavus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.32 2.38
-
 phosphatidic acid pH 7.2, 50°C, recombinant enzyme Streptomyces albidoflavus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.1.32 additional information the enzyme possesses a 33-residue N-terminal signal secretion sequence Streptomyces albidoflavus
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.32 Ca2+ activates at 10 mM Streptomyces albidoflavus
3.1.1.32 additional information metal ion-independent phospholipase A1 Streptomyces albidoflavus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.32 27199
-
 1 * 27199, mature protein, seuence calculation, 1 * 28000, recombinant extracellular enzyme, SDS-PAGE Streptomyces albidoflavus
3.1.1.32 28000
-
 DLS analysis Streptomyces albidoflavus

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.32 Streptomyces albidoflavus K0J3J2 isolated from Japanese soil, gene pla
-
3.1.1.32 Streptomyces albidoflavus NA297 K0J3J2 isolated from Japanese soil, gene pla
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.32 recombinant extracellular enzyme to homogeneity from the culture supernatant by ammonium sulfate precipitation, hydrophobic interaction chromatography, and anion exchange chromatography Streptomyces albidoflavus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.1.32 588 2873 pH 7.2, 50°C, purified recombinant enzyme Streptomyces albidoflavus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.32 1,2-dimyristoyl-sn-glycero-3-phosphate + H2O
-
 Streptomyces albidoflavus ?
-
 ?
3.1.1.32 1,2-dimyristoyl-sn-glycero-3-phosphate + H2O
-
 Streptomyces albidoflavus NA297 ?
-
 ?
3.1.1.32 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine + H2O
-
 Streptomyces albidoflavus ?
-
 ?
3.1.1.32 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine + H2O
-
 Streptomyces albidoflavus NA297 ?
-
 ?
3.1.1.32 1,2-dipalmitoyl-sn-glycero-3-phosphocholine + H2O
-
 Streptomyces albidoflavus ?
-
 ?
3.1.1.32 1,2-dipalmitoyl-sn-glycero-3-phosphocholine + H2O
-
 Streptomyces albidoflavus NA297 ?
-
 ?
3.1.1.32 L-alpha-phosphatidyl-L-serine + H2O substrate from Glycine max Streptomyces albidoflavus 2-acyl-1-glycerophosphoserine + a carboxylate
-
 ?
3.1.1.32 L-alpha-phosphatidylcholine + H2O PLA1 activity for egg yolk lecithin hydrolysis, substrate from egg yolk or Glycine max Streptomyces albidoflavus 2-acylglycerophosphocholine + a carboxylate
-
 ?
3.1.1.32 L-alpha-phosphatidylglycerol + H2O
-
 Streptomyces albidoflavus ?
-
 ?
3.1.1.32 L-alpha-phosphatidylinositol + H2O
-
 Streptomyces albidoflavus 2-acyl-sn-glycero-3-phosphoinositol + a carboxylate
-
 ?
3.1.1.32 lecithin + H2O from Glycine max Streptomyces albidoflavus ?
-
 ?
3.1.1.32 additional information the substrate specificity is pH-dependent, the enzyme preferably hydrolyzes phosphatidic acid and phosphatidylserine at pH 7.2, it is active with lysophosphatidylcholine, but not with triglyceride and the 4-nitrophenyl ester of fatty acids, substrate specificity, overview. At the reaction equilibrium, the molar ratio of released free fatty acids (sn-1:sn-2) is 63:37 Streptomyces albidoflavus ?
-
 ?
3.1.1.32 additional information the substrate specificity is pH-dependent, the enzyme preferably hydrolyzes phosphatidic acid and phosphatidylserine at pH 7.2, it is active with lysophosphatidylcholine, but not with triglyceride and the 4-nitrophenyl ester of fatty acids, substrate specificity, overview. At the reaction equilibrium, the molar ratio of released free fatty acids (sn-1:sn-2) is 63:37 Streptomyces albidoflavus NA297 ?
-
 ?
3.1.1.32 phosphatidic acid + H2O
-
 Streptomyces albidoflavus 2-acyl-lysophosphatidic acid + a carboxylate
-
 ?
3.1.1.32 phosphatidic acid + H2O
-
 Streptomyces albidoflavus NA297 2-acyl-lysophosphatidic acid + a carboxylate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.1.32 monomer 1 * 27199, mature protein, seuence calculation, 1 * 28000, recombinant extracellular enzyme, SDS-PAGE Streptomyces albidoflavus

Synonyms

EC Number Synonyms Comment Organism
3.1.1.32 PLA1
-
 Streptomyces albidoflavus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.32 50
-
-
 Streptomyces albidoflavus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.1.1.32 20 70 activity range, profile overview Streptomyces albidoflavus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.32 40
-
 native and recombinant enzymes, stable at Streptomyces albidoflavus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.1.32 630
-
 phosphatidic acid pH 7.2, 50°C, recombinant enzyme Streptomyces albidoflavus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.32 7.2
-
-
 Streptomyces albidoflavus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.1.32 4 11 activity range, profile overview Streptomyces albidoflavus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.1.1.32 5.6 9 recombinant enzyme, stable at Streptomyces albidoflavus
3.1.1.32 7.2 9 native enzyme, stable at Streptomyces albidoflavus

General Information

EC Number General Information Comment Organism
3.1.1.32 additional information residue Ser11 is essential for the catalytic function of the enzyme, the active site may include residues Ser216 and His218 Streptomyces albidoflavus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.1.1.32 265
-
 phosphatidic acid pH 7.2, 50°C, recombinant enzyme Streptomyces albidoflavus