Lysyl oxidase (LOX) is an amine oxidase metalloenzyme that catalyzes the oxidation of peptidyl amines in lysine residues to α-aminoadipic-δ-semialdehydes in its macromolecule substrates, collagen and elastin, giving the extra cellular matrix its characteristic strength, and flexibility. Recent research data has made it apparent that LOX plays a crucial role in many normal and disease related cell functions making this intriguing enzyme of high interest and importance for further studies. Additional studies are necessary to understand more about LOX’s unknown characteristics such as its exact role in cellular functions, the role of LOX’s Cu(II) co-factor in its catalytic mechanism, its 3-dimensional structure, and interactions with its selective inhibitor B-aminopropionitrile (BAPN) . The main purpose of this investigation is to identify and chemically modify amino acid residues thought to be important in the catalytic mechanism of LOX. An optimized method of purification recently developed by our research group has allowed us to obtain the pure active LOX in sufficient yield, purity, and activity, appropriate for further characterization. <i>In silico</i> experiments have identified amino acid residues that may be essential in LOX’s catalytic mechanism including glutamine, aspartic acid, histidine and arginine. Chemical modifications of these identified residues were then performed in accordance with molecular modeling results to explore their role in LOX’s enzymatic activity. The roles of these identified residues in LOX’s catalytic mechanism are discussed.

Chemical modifications of catalytically important residues of enzyme lysyl oxidase

249th National Meeting (2015)

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