Any feedback?
Literature summary for 3.1.1.32 extracted from
- Purification, characterization, molecular cloning and extracellular production of a phospholipase A1 from Streptomyces albidoflavus NA297 (2012), FEBS open bio, 2, 318-327.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| 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
| Protein Variants | Comment | Organism |
|---|---|---|
| H218A | site-directed mutagenesis, inactive mutant | Streptomyces albidoflavus |
| H218R | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Streptomyces albidoflavus |
| S11A | site-directed mutagenesis, inactive mutant | Streptomyces albidoflavus |
| S11D | site-directed mutagenesis, inactive mutant | Streptomyces albidoflavus |
| S11E | site-directed mutagenesis, inactive mutant | Streptomyces albidoflavus |
| S11T | site-directed mutagenesis, inactive mutant | Streptomyces albidoflavus |
| S11Y | site-directed mutagenesis, inactive mutant | Streptomyces albidoflavus |
| S216A | site-directed mutagenesis, inactive mutant | Streptomyces albidoflavus |
| S216D | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Streptomyces albidoflavus |
| S216E | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Streptomyces albidoflavus |
| S216T | site-directed mutagenesis, the mutant shows 80-90% reduced activity compared to the wild-type enzyme | Streptomyces albidoflavus |
| S216Y | site-directed mutagenesis, the mutant shows 80-90% reduced activity compared to the wild-type enzyme | Streptomyces albidoflavus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 2-mercaptoethanol | weak inhibition | Streptomyces albidoflavus |  |
| Ca2+ | up to 0.1 mM | Streptomyces albidoflavus | |
| Fe2+ | - |
Streptomyces albidoflavus | |
| Fe3+ | - |
Streptomyces albidoflavus | |
| additional information | the enzyme is not inhibited by EDTA and DTT | Streptomyces albidoflavus | |
| PMSF | weak inhibition | Streptomyces albidoflavus | |
| SDS | - |
Streptomyces albidoflavus | |
| Triton X-100 | weak inhibition at up to 0.23% w/v | Streptomyces albidoflavus | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 2.38 | - |
phosphatidic acid | pH 7.2, 50°C, recombinant enzyme | Streptomyces albidoflavus | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| additional information | the enzyme possesses a 33-residue N-terminal signal secretion sequence | Streptomyces albidoflavus | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | activates at 10 mM | Streptomyces albidoflavus | |
| additional information | metal ion-independent phospholipase A1 | Streptomyces albidoflavus |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 27199 | - |
1 * 27199, mature protein, seuence calculation, 1 * 28000, recombinant extracellular enzyme, SDS-PAGE | Streptomyces albidoflavus |
| 28000 | - |
DLS analysis | Streptomyces albidoflavus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Streptomyces albidoflavus | K0J3J2 | isolated from Japanese soil, gene pla | - |
| Streptomyces albidoflavus NA297 | K0J3J2 | isolated from Japanese soil, gene pla | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| 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]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 588 | 2873 | pH 7.2, 50°C, purified recombinant enzyme | Streptomyces albidoflavus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 1,2-dimyristoyl-sn-glycero-3-phosphate + H2O | - |
Streptomyces albidoflavus | ? | - |
? | |
| 1,2-dimyristoyl-sn-glycero-3-phosphate + H2O | - |
Streptomyces albidoflavus NA297 | ? | - |
? | |
| 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine + H2O | - |
Streptomyces albidoflavus | ? | - |
? | |
| 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine + H2O | - |
Streptomyces albidoflavus NA297 | ? | - |
? | |
| 1,2-dipalmitoyl-sn-glycero-3-phosphocholine + H2O | - |
Streptomyces albidoflavus | ? | - |
? | |
| 1,2-dipalmitoyl-sn-glycero-3-phosphocholine + H2O | - |
Streptomyces albidoflavus NA297 | ? | - |
? | |
| L-alpha-phosphatidyl-L-serine + H2O | substrate from Glycine max | Streptomyces albidoflavus | 2-acyl-1-glycerophosphoserine + a carboxylate | - |
? | |
| L-alpha-phosphatidylcholine + H2O | PLA1 activity for egg yolk lecithin hydrolysis, substrate from egg yolk or Glycine max | Streptomyces albidoflavus | 2-acylglycerophosphocholine + a carboxylate | - |
? | |
| L-alpha-phosphatidylglycerol + H2O | - |
Streptomyces albidoflavus | ? | - |
? | |
| L-alpha-phosphatidylinositol + H2O | - |
Streptomyces albidoflavus | 2-acyl-sn-glycero-3-phosphoinositol + a carboxylate | - |
? | |
| lecithin + H2O | from Glycine max | Streptomyces albidoflavus | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| phosphatidic acid + H2O | - |
Streptomyces albidoflavus | 2-acyl-lysophosphatidic acid + a carboxylate | - |
? | |
| phosphatidic acid + H2O | - |
Streptomyces albidoflavus NA297 | 2-acyl-lysophosphatidic acid + a carboxylate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 27199, mature protein, seuence calculation, 1 * 28000, recombinant extracellular enzyme, SDS-PAGE | Streptomyces albidoflavus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PLA1 | - |
Streptomyces albidoflavus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
- |
Streptomyces albidoflavus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | 70 | activity range, profile overview | Streptomyces albidoflavus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
native and recombinant enzymes, stable at | Streptomyces albidoflavus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 630 | - |
phosphatidic acid | pH 7.2, 50°C, recombinant enzyme | Streptomyces albidoflavus | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | - |
- |
Streptomyces albidoflavus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 11 | activity range, profile overview | Streptomyces albidoflavus |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 5.6 | 9 | recombinant enzyme, stable at | Streptomyces albidoflavus |
| 7.2 | 9 | native enzyme, stable at | Streptomyces albidoflavus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 265 | - |
phosphatidic acid | pH 7.2, 50°C, recombinant enzyme | Streptomyces albidoflavus | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
