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Literature summary for 4.6.1.13 extracted from

  • Ryan, M.; Liu, T.; Dahlquist, F.W.; Griffith, O.H.
    A catalytic diad involved in substrate-assisted catalysis: NMR study of hydrogen bonding and dynamics at the active site of phosphatidylinositol-specific phospholipase C (2001), Biochemistry, 40, 9743-9750.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Bacillus cereus

Crystallization (Commentary)

Crystallization (Comment) Organism
X-ray crystal structure Bacillus cereus

Protein Variants

Protein Variants Comment Organism
D274A mutation of an catalytic diad residue, mutant with abolished activity, NMR study Bacillus cereus
D274N mutation of an catalytic diad residue, 4.2% of wild-type activity Bacillus cereus
H32A mutation of an catalytic diad residue, mutant with abolished activity, NMR study Bacillus cereus

Organism

Organism UniProt Comment Textmining
Bacillus cereus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant PI-PLC Bacillus cereus

Reaction

Reaction Comment Organism Reaction ID
1-phosphatidyl-1D-myo-inositol = 1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol mechanism Bacillus cereus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-phosphatidyl-1D-myo-inositol a catalytic diad at the active site composed of Asp-274 and His-32 is involved in substrate-assisted catalysis, its function is to hydrogen-bond with the 2-OH of phosphatidylinositol to form a catalytic triad, catalytic mechanism Bacillus cereus 1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol PI-PLC catalyzes in a second step the slow hydrolysis of 1D-myo-inositol 1,2-cyclic phosphate to form myo-inositol 1-phosphate ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Bacillus cereus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Bacillus cereus