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Book of Abstracts: Albany 2009

category image Albany 2009
Conversation 16
June 16-20 2009
© Adenine Press (2008)

Investigation of Natural and Selected Nucleic Acid Enzymes that Depend on Coenzymes

The glmS riboswitch occurs in all gram-positive bacteria exerting feedback control over production of glucosamine-6-phosphate (GlcN6P) that is used towards cell-wall synthesis. Recent biochemical and structural analyses suggest that the GlcN6P cofactor acts as a coenzyme; GlcN6P binds to the RNA and acts directly to catalyze RNA cleavage. Through analyses of the cleavage reaction with normal and hyperactivated 5'-S-phosphorothiolate substrates as well as GlcN6P analogues, we investigate the mechanistic role of the putative GlcN6P coenzyme. In addition, to determine the effectiveness of a GlcN6P cofactor in catalysis of RNA cleavage we are using in vitro selection methods to identify GlcN6P-dependent DNAzymes. We seek to compare the cleavage mechanism of the GlcN6P-dependent DNAzyme to that of the natural glmS ribozyme as well as other selected DNAzymes that putatively use a coenzyme. While protein enzymes are well known to use coenzymes, the use of coenzymes maybe a hitherto underestimated catalytic strategy among nucleic acid enzymes

Subha Das
Eduardo Paredes

Department of Chemistry
Carnegie Mellon University
Pittsburgh, PA 15213 USA
srdas@andrew.cmu.edu