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Literature summary extracted from

  • Masayama, A.; Takahashi, T.; Tsukada, K.; Nishikawa, S.; Takahashi, R.; Adachi, M.; Koga, K.; Suzuki, A.; Yamane, T.; Nakano, H.; Iwasaki, Y.
    Streptomyces phospholipase D mutants with altered substrate specificity capable of phosphatidylinositol synthesis (2008), ChemBioChem, 9, 974-981.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.4.4 expressed in Escherichia coli Streptomyces antibioticus
3.1.4.4 mutants are expressed in Escherichia coli Streptomyces antibioticus

Protein Variants

EC Number Protein Variants Comment Organism
3.1.4.4 H168A inactive Streptomyces antibioticus
3.1.4.4 additional information the phosphatidylcholine-hydrolyzing activity of the mutant PLD 187F/191R/385Y is much lower than that of the wild-type enzyme, the mutant enzyme is able to transphosphatidylate various cyclohexanols with a preference for bulkier compounds Streptomyces antibioticus
3.1.4.4 W187F/Y191R mutant enzyme is able to synthesize phosphatidylinositol using dioleoyl-phosphatidylcholine and myo-inositol as a substrate, the mutant enzyme generates a mixture of structural isomers of phosphatidylinositol with the phosphatidyl groups connected at different positions of the inositol ring. In the cases of 1,2-diols, triols, and myo-inositol mutant W187F/Y191R generates the corresponding transphosphatidylated products more efficiently than wild-type. The phosphatidylcholine-hydrolyzing activity of the mutant PLD is much lower than that of the wild-type enzyme (Km higher, Vmax much lower than wild-type). Mutant enzyme is able to transphosphatidylate various cyclohexanols with a preference for bulkier compounds Streptomyces antibioticus
3.1.4.4 W187X/Y191X/Y385X mutations are introduced in the pld gene at the positions corresponding to three amino acid residues that might be involved in substrate recognition, and the mutated genes are expressed in Escherichia coli. High-throughput screening of approximately 10000 colonies for phosphatidylinositol-synthesizing activity identifies 25 phosphatidylinositol-synthesizing mutant PLDs Streptomyces antibioticus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.4.4 0.0015
-
dioleoyl-phosphatidylcholine wild type enzyme, in sodium acetate buffer (50 mM, pH 5.6), at 37°C Streptomyces antibioticus
3.1.4.4 0.003
-
dioleoyl-phosphatidylcholine mutant enzyme 187F/191R/385Y, in sodium acetate buffer (50 mM, pH 5.6), at 37°C Streptomyces antibioticus
3.1.4.4 1.5
-
dioleoyl-phosphatidylcholine wild-type, Vmax: 4700 micromol/min/mg Streptomyces antibioticus
3.1.4.4 3
-
dioleoyl-phosphatidylcholine mutant W187F/Y191R, Vmax: 1.8 micromol/min/mg Streptomyces antibioticus

Organism

EC Number Organism UniProt Comment Textmining
3.1.4.4 Streptomyces antibioticus
-
-
-
3.1.4.4 Streptomyces antibioticus Q53728
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.4.4 dioleoyl-phosphatidylcholine + cyclohexane-1,2,3-triol in the cases of 1,2-diols, triols, and myo-inositol mutant W187F/Y191R generates the corresponding transphosphatidylated products more efficiently than wild-type Streptomyces antibioticus choline + dioleoyl-phosphatidylcyclohexane-2,3-diol
-
?
3.1.4.4 dioleoyl-phosphatidylcholine + cyclohexane-1,2,5-triol in the cases of 1,2-diols, triols, and myo-inositol mutant W187F/Y191R generates the corresponding transphosphatidylated products more efficiently than wild-type Streptomyces antibioticus choline + dioleoyl-phosphatidylcyclohexane-2,5-diol
-
?
3.1.4.4 dioleoyl-phosphatidylcholine + cyclohexane-1,2-diol in the cases of 1,2-diols, triols, and myo-inositol mutant W187F/Y191R generates the corresponding transphosphatidylated products more efficiently than wild-type Streptomyces antibioticus choline + dioleoyl-phosphatidylcyclohexane-2-ol
-
?
3.1.4.4 dioleoyl-phosphatidylcholine + cyclohexane-1,3-diol in the cases of 1,2-diols, triols, and myo-inositol mutant W187F/Y191R generates the corresponding transphosphatidylated products more efficiently than wild-type Streptomyces antibioticus choline + dioleoyl-phosphatidylcyclohexane-3-ol
-
?
3.1.4.4 dioleoyl-phosphatidylcholine + cyclohexane-1,4-diol
-
Streptomyces antibioticus choline + dioleoyl-phosphatidylcyclohexane-4-ol
-
?
3.1.4.4 dioleoyl-phosphatidylcholine + cyclohexanol in the cases of cyclohexanol and of cyclohexane-1,4-diol, the wild-type enzyme generates the corresponding transphosphatidylated products more efficiently than the mutant W187F/Y191R Streptomyces antibioticus choline + dioleoyl-phosphatidylcyclohexane
-
?
3.1.4.4 dioleoyl-phosphatidylcholine + H2O
-
Streptomyces antibioticus choline + dioleoyl-phosphatidate
-
?
3.1.4.4 dioleoyl-phosphatidylcholine + myo-inositol in the cases of 1,2-diols, triols, and myo-inositol mutant W187F/Y191R generates the corresponding transphosphatidylated products more efficiently than wild-type Streptomyces antibioticus ?
-
?
3.1.4.4 dioleoyl-phosphatidylcholine + myo-inositol
-
Streptomyces antibioticus phosphatidylinositol + choline the FRY mutant generates 1(3)-phosphatidylinositol and 4(6)-phosphatidylinositol, but not 2-phosphatidylinositol and 5-phosphatidylinositol ?
3.1.4.4 phospholipid + H2O
-
Streptomyces antibioticus phosphatidic acid + alcohol
-
?

Synonyms

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