Work

Trans-Cyclization of Phosphatidylinositol Catalyzed by Phospholipase C from Streptomyces antibioticus

Year: 2009

Type: article

Abstract: Calcium-dependent phosphatidylinositol-specific phospholipase C from Streptomyces antibioticus (saPLC1) catalyzes the cleavage of phosphatidylinositol (PI) by an unusual mechanism involving a 1,6-cyclization with formation of inositol trans-1,6-cyclic phosphate (1,6-IcP), rather then inositol cis-1,2-cyclic phosphate (1,2-IcP). This conclusion has been reached based on the comparison of the released cyclic phosphate intermediate by the H16A mutant of saPLC1 with a genuine 1,6-IcP synthesized by a chemoenzymatic approach.

Source: Journal of the American Chemical Society

DOI: 10.1021/ja902326u

Authors: Chuan Bai, Li Zhao, Mario Rebecchi, Ming-Daw Tsai, Karol S. Bruzik

Institutions: University of Illinois Chicago, The Ohio State University, Stony Brook University, Academia Sinica

Language: English

Topic: Protein Kinase Regulation and GTPase Signaling

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funder: National Institute of General Medical Sciences

Awards: G2436395368, Mechanism of Calcium-Dependent Phospholipases C