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Advisor(s)
Abstract(s)
The interaction of a variety of substrates with Pseudomonas aeruginosa native amidase (E.C. 3.5.1.4), overproduced in an Escherichia coli strain, was investigated using difference FTIR spectroscopy. The amides used as substrates showed an increase in hydrogen bonding upon association in multimers, which was not seen with esters. Evidence for an overall reduction or weakening of hydrogen bonding while amide and ester substrates are interacting with the enzyme is presented. The results describe a spectroscopic approach for analysis of substrate-amidase interaction and in situ monitoring of the hydrolysis and transferase reaction when amides or esters are used as substrates.
Description
Keywords
Recombinant Amidase Difference FTIR spectroscopy Substrates interaction Catalytic mechanism Transform infrared-spectroscopy Human serum-albumin Molecular interpretation Difference spectra Enzymatic-activity Active-site Binding FTIR ATP Hydrolysis
Citation
Pacheco R, Karmali A, Serralheiro M L M, Haris P I. Substrate interaction with recombinant amidase from Pseudomonas aeruginosa during biocatalysis. Biocatalys and Biotransformation. 2009; 27 (5-6): 367-376.