Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.6.1.13 extracted from

  • Itami, C.; Kimura, Y.; Taguchi, R.; Ikezawa, H.; Nakayashi, T.
    Growth inhibition, morphological change, and ectoenzyme release of LLC-PK1 cells by phosphatidylinositol-specific phospholipase C of Bacillus thuringiensis (1997), Biosci. Biotechnol. Biochem., 61, 776-781.
    View publication on PubMed

Application

Application Comment Organism
analysis use of the enzyme and specific antibodies for the enzyme for the examination of the growth inhibition, morphological change and ectoenzyme release of the LLC-PK1 cells from pig, effective for the investigation of the function of the glycosyl-phosphatidylinositol-anchor protein Bacillus thuringiensis

Organism

Organism UniProt Comment Textmining
Bacillus thuringiensis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information approximately 20% of the alkaline phosphodiesterase I activity is released from the apical surface of the pig LLC-PK1 cells by the action of the 1-phosphatidylinositol phosphodiesterase Bacillus thuringiensis ?
-
?
phosphatidylinositol + H2O
-
Bacillus thuringiensis diacylglycerol + myo-inositol 1,2-cyclic phosphate
-
?