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Slow Solvation Dynamics at the Active Site of an Enzyme: Implications for Catalysis

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Title Slow Solvation Dynamics at the Active Site of an Enzyme: Implications for Catalysis
 
Creator Guha, Soumi
Sahu, Kalyanasis
Roy, Durba
Mondal, Sudip Kumar
Roy, Siddhartha
Bhattacharyya, Kankan
 
Subject Structural Biology & Bioinformatics
 
Description Solvation dynamics at the active site of an enzyme, glutaminyl-tRNA synthetase (GlnRS),
was studied using a fluorescence probe, acrylodan, site-specifically attached at cysteine residue C229,
near the active site. The picosecond time-dependent fluorescence Stokes shift indicates slow solvation
dynamics at the active site of the enzyme, in the absence of any substrate. The solvation dynamics becomes
still slower when the substrate (glutamine or tRNAGln) binds to the enzyme. A mutant Y211H-GlnRS
was constructed in which the glutamine binding site is disrupted. The mutant Y211H-GlnRS labeled at
C229 with acrylodan exhibited significantly different solvent relaxation, thus demonstrating that the slow
dynamics is indeed associated with the active site. Implications for catalysis and specificity have been
discussed.
 
Date 2005
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://www.eprints.iicb.res.in/1082/1/BIOCHEMISTRY%2C_44(_25)%2C__8940%2D8947_[51].pdf
Guha, Soumi and Sahu, Kalyanasis and Roy, Durba and Mondal, Sudip Kumar and Roy, Siddhartha and Bhattacharyya, Kankan (2005) Slow Solvation Dynamics at the Active Site of an Enzyme: Implications for Catalysis. Biochemistry, 44 (25). pp. 8940-8947.
 
Relation http://dx.doi.org/10.1021/bi0473915
http://www.eprints.iicb.res.in/1082/