Lysyl oxidase (LOX, EC 1.4.3.13) is a copper-dependent enzyme involved in many biological processes.  Due to its low solubility, very little is known about the structure of this enzyme.  In an effort to further characterize this enzyme, the five histidine residues located in the putative copper-binding region were mutated to alanine and the enzymatic activity of each mutant was monitored using established assays.  Copper content, secondary structure content, and redox-cycling activity were also monitored.  In all cases, the enzyme appears to fold correctly; however, the copper content, enzymatic activity, and redox cycling activity were mutant dependent.  Based on the data collected, His292, His294, and His 296 were determined to be the copper-binding residues in LOX.  The other two residues in the copper-binding region (His289 and His303) appear to play no role in copper-binding.

Identification of the copper-binding ligand in human lysyl oxidase

243rd National Meeting (2012)

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