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Literature summary extracted from

  • Damnjanovic, J.; Takahashi, R.; Suzuki, A.; Nakano, H.; Iwasaki, Y.
    Improving thermostability of phosphatidylinositol-synthesizing Streptomyces phospholipase D (2012), Protein Eng. Des. Sel., 25, 415-424.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.4.4 expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha-FT Streptomyces antibioticus

Protein Variants

EC Number Protein Variants Comment Organism
3.1.4.4 D40H/W187D/Y191Y/R329G/Y385R random mutagenesis of mutant W187D/Y191Y/Y385R, the resulting mutant shows increased thermostability compared to the wild-type enzyme and transphosphatidylation with myo-inositol and phosphocholine Streptomyces antibioticus
3.1.4.4 D40H/W187D/Y191Y/T291Y/R329G/Y385R random mutagenesis of mutant W187D/Y191Y/Y385R, the resulting mutant shows increased thermostability compared to the wild-type enzyme and transphosphatidylation with myo-inositol and phosphocholine Streptomyces antibioticus
3.1.4.4 D40H/W187D/Y191Y/T291Y/Y385R random mutagenesis of mutant W187D/Y191Y/Y385R, the resulting mutant shows increased thermostability compared to the wild-type enzyme and transphosphatidylation with myo-inositol and phosphocholine Streptomyces antibioticus
3.1.4.4 additional information increased thermostability of mutant enzymes, especially those with D40H/T291Y mutation, compared to the wild-type enzyme, molecular dynamics analysis and molecular dynamics simulation, overview Streptomyces antibioticus
3.1.4.4 W187D/Y191Y/T291Y/R329G/Y385R random mutagenesis of mutant W187D/Y191Y/Y385R, the resulting mutant shows increased thermostability compared to the wild-type enzyme and transphosphatidylation with myo-inositol and phosphocholine Streptomyces antibioticus
3.1.4.4 W187D/Y191Y/Y385R site-directed mutagenesis, the mutant synthesizes phosphatidylinositol from myo-inositol and phosphocholine by transphosphatidylation Streptomyces antibioticus

Organism

EC Number Organism UniProt Comment Textmining
3.1.4.4 Streptomyces antibioticus Q53728
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-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.4.4 0.0204 0.0233 transphosphatidylation activities of mutant enzmes, pH 5.6, 30°C Streptomyces antibioticus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.4.4 dioleoylphosphatidylcholine + myo-inositol transphosphatidylation activity of mutant W187D/Y191Y/Y385R enzyme Streptomyces antibioticus choline + dioleoylphosphatidylinositol
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.4.4 phosphatidylinositol-synthesizing phospholipase D
-
 Streptomyces antibioticus
3.1.4.4 PLD
-
 Streptomyces antibioticus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.4.4 30
-
 assay at Streptomyces antibioticus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.4.4 65
-
 increased thermostability of mutant enzymes, especially those with D40H/T291Y mutation, compared to the wild-type enzyme, half-lives lie between 20 and 40 min, molecular dynamics analysis and molecular dynamics simulation, overview Streptomyces antibioticus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.4.4 5.6
-
 assay at Streptomyces antibioticus