Role of side-edge site of sphingomyelinase from Bacillus cereus

Biochemical and Biophysical Research Communications
Masataka OdaJun Sakurai

Abstract

Bacillus cereus sphingomyelinase (Bc-SMase) belongs to the Mg(2+)-dependent neutral sphingomyelinase (nSMase) which hydrolyzes sphingomyelin (SM) to produce phosphocholine and ceramide, and acts as an extracellular hemolysin. Bc-SMase has two metal ion-binding sites in a long horizontal cleft across the molecule, with one Mg(2+) in the central region of the cleft and one divalent metal ion at the side-edge of the cleft. The role of the Mg(2+) at the side-edge of the long horizontal cleft in Bc-SMase remains unresolved. The replacement of Asn-57, Glu-99, and Asp-100 located in close proximity to Mg(2+) at the side-edge with alanine resulted in a striking reduction in binding to and hydrolysis of sphingomyelin in membranes of sheep erythrocytes or SM-liposomes but that of Phe-55 did not. However, the replacement of these residues had little effect on the enzymatic activity. N57A, E99A, and D100A contained 2 mol of Mg(2+) per mol of protein, and the wild type and F55A contained 3 mol. A crystal analysis showed that N57A with Mg(2+) had no metal ion at the side-edge. These results indicate that the Mg(2+) at the side-edge of Bc-SMase plays an important role in the binding to membranes.

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Mar 11, 2010·Biochimica Et Biophysica Acta·Masataka OdaJun Sakurai

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Citations

Mar 16, 2013·Journal of Enzyme Inhibition and Medicinal Chemistry·Masataka OdaMasahiro Nagahama
Jan 15, 2013·Biochemical and Biophysical Research Communications·Masataka OdaMasahiro Nagahama
Feb 6, 2020·Biological & Pharmaceutical Bulletin·Masataka OdaGo Kamoshida

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