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Literature summary for 4.6.1.13 extracted from
- Unique catalytic mechanism of phosphatidylinositol-specific phospholipase C from Streptomyces antibioticus (2010), J. Am. Chem. Soc., 132, 1210-1211.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Streptomyces antibioticus | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| dihexanoylphosphatidyl inositol | - |
Streptomyces antibioticus | ? | - |
? |  |
| dihexanoylphosphorothioyl-myo-inositol | - |
Streptomyces antibioticus | myo-inositol cis(2-OH,S)-1,6-cyclic phosphorothioate + 1,2-dihexanoyl-sn-glycerol | - |
? | |
| additional information | synthesis of short-chain (dihexanoyl) analogues of phosphatidylinositol as substrates. The intermediate is generated from dihexanoylphosphorothioyl-myo-inositol identified as myo-inositol cis(2-OH,S)-1,6-cyclic phosphorothioate. The cyclic intermediate is gradually hydrolyzed to inositol 1-phosphorothioate. Both the Rp and Sp isomers of the phosphorodithioate analogue are readily cleaved, with the Sp isomer being hydrolyzed only ca. 6times more slowly than the Rp isomer. Rates of cleavage of two other substrates in which the pro-S oxygen is left unaltered, dihexanoylphosphorothioyl-myo-inositol and dihexanoylphosphatidyl inositol, are affected to only a small extent (0.6 and 1.6-fold, respectively) by the analogous modification of the bridging position. Strong Sp thio effect arises from a loss of a catalytic interaction rather than a steric effect | Streptomyces antibioticus | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| phosphatidylinositol-specific phospholipase C | - |
Streptomyces antibioticus |
| PLC1 | - |
Streptomyces antibioticus |
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