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Literature summary for 3.1.4.4 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
Search for more literature for 3.1.4.4

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
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
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
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
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
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
W187D/Y191Y/Y385R site-directed mutagenesis, the mutant synthesizes phosphatidylinositol from myo-inositol and phosphocholine by transphosphatidylation Streptomyces antibioticus

Organism

Organism UniProt Comment Textmining
Streptomyces antibioticus Q53728
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-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
phosphatidylinositol-synthesizing phospholipase D
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 Streptomyces antibioticus
PLD
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 Streptomyces antibioticus

Temperature Optimum [°C]

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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

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