Trans-cyclization of phosphatidylinositol catalyzed by phospholipase C from Streptomyces antibioticus.
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.
Bai
Chuan
C
Department of Medicinal Chemistry and Pharmacognosy, The University of Illinois at Chicago, Chicago, Illinois 60612, USA.
Zhao
Li
L
Rebecchi
Mario
M
Tsai
Ming-Daw
MD
Bruzik
Karol S
KS
D002384:Catalysis; D003500:Cyclization; D019906:Nuclear Magnetic Resonance, Biomolecular; D010716:Phosphatidylinositols / Q000737:chemistry / Q000378:metabolism*; D013303:Streptomyces antibioticus / Q000201:enzymology*; D013379:Substrate Specificity; D010738:Type C Phospholipases / Q000737:chemistry / Q000378:metabolism*
D010716:Phosphatidylinositols; D010738:Type C Phospholipases