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Literature summary for 4.6.1.13 extracted from

  • Guo, S.; Zhang, X.; Seaton, B.A.; Roberts, M.F.
    Role of helix B residues in interfacial activation of a bacterial phosphatidylinositol-specific phospholipase C (2008), Biochemistry, 47, 4201-4210.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
phosphatidylcholine
-
Bacillus thuringiensis

Cloned(Commentary)

Cloned (Comment) Organism
transformed into Escherichia coli BL21-Codonplus (DE3)-RIL cells Bacillus thuringiensis

Protein Variants

Protein Variants Comment Organism
G48A single mutant Bacillus thuringiensis
I43A single mutant Bacillus thuringiensis
I43W single mutant Bacillus thuringiensis
I43W/W47I are made by introducing the second mutation in the gene coding for a single mutant Bacillus thuringiensis
K44E single mutant Bacillus thuringiensis
L39A single mutant Bacillus thuringiensis
L39A/V46A are made by introducing the second mutation in the gene coding for a single mutant Bacillus thuringiensis
P42G single mutant Bacillus thuringiensis
Q45A single mutant Bacillus thuringiensis
V46A single mutant Bacillus thuringiensis
W47A/W242A dimeric mutant, which is unable to bind to phosphatidycholine Bacillus thuringiensis

Organism

Organism UniProt Comment Textmining
Bacillus thuringiensis P08954
-
-

Purification (Commentary)

Purification (Comment) Organism
Q-sepharose fast-flow column and phenyl-Sepharose column, monitored by SDS-PAGE Bacillus thuringiensis

Subunits

Subunits Comment Organism
monomer although small amounts of dimer have been noted previously Bacillus thuringiensis

Synonyms

Synonyms Comment Organism
phosphatidylinositol-specific phospholipase C
-
Bacillus thuringiensis
PI-PLC
-
Bacillus thuringiensis