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. Author manuscript; available in PMC: 2009 Nov 1.
Published in final edited form as: Mol Genet Metab. 2008 Sep 23;95(3):152–162. doi: 10.1016/j.ymgme.2008.08.004

Fig. 4. Protein alignment of ASM with lysenin and phospholipases A2 and C.

Fig. 4

Sequences were extracted from the SWISSPROT database and the Protein Data Bank (PDB), and aligned using ClustalW (Version 1.7). (A) Predicted substrate binding site of ASM aligned with lysenin (LYS). Numbers above the ASM sequence indicate the position of the amino acids in the ASM protein. Asterisks under the sequence represent amino acids bearing similar biochemical properties. (B) Predicted active site of ASM aligned with phospholipase C (PLC). Numbers above the ASM sequence indicate the position of the amino acids in the ASM protein. Asterisks under the sequence represent amino acids bearing similar biochemical properties. Colons under the sequence represent conserved histidine residues involved in metal binding. (C) Homology between ASM and the predicted active site region of phospholipase A2 (PA2). The underlined area indicates the critical active site region of phospholipase A2. Numbers above the ASM sequence indicate the position of the amino acids in the ASM protein. Asterisks under the sequence represent amino acids bearing similar biochemical properties.