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 |
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 |
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 |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.4.4 | Streptomyces antibioticus | - |
- |
- |
3.1.4.4 | Streptomyces antibioticus | Q53728 | - |
- |
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 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.4.4 | phospholipase D | - |
Streptomyces antibioticus |
3.1.4.4 | PLD | - |
Streptomyces antibioticus |