COMP 15 |
| Pranav Dalal1, Jeffry D. Madura1, and Nathan N. Aronson Jr.2. (1) Department of Chemistry and Biochemistry, Center for Computational Sciences, Duquesne University, 600 Forbes Avenue, Pittsburgh, PA 15226, (2) Department of Biochemistry and Molecular Biology, Univ. of South Alabamda, University of South Alabama, 307 University Blvd., Mobile, AL 36688 |
| Glycosidases and lectins both bind sugars, but only the glycosidases are catalytic. The glycosidases occur among 90 evolved protein families. Family 18 is one of the two familes of chitinases (EC 3,2.1.14). Interestingly, lectins are also in this evolutionary group of Family 18 glycosidase proteins. Proteins belonging to the enzymatically inactive class ("chitolectins") have a highly similar binding site to the catalytic Family 18 enzymes. One major exception is a glutamic acid which acts as the essential acid/base residue for chitin cleavage is replaced with leucine or glutamine. We present our comparison of the recently obtained structures of two Family 18 chitolectins, MGP40 (Mohanty, Singh et al., 2003) and GP39 (Fusetti, Pijning et al., 2003; Houston, Anneliese et al., 2003). |
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Computers in Chemistry General
8:20 AM-12:20 PM, Sunday, August 22, 2004 Pennsylvania Convention Center -- 104A&B, Oral
Division of Computers in Chemistry |