Oxidation of tryptophan in lysozyme by ozone in aqueous solution.
A tryptophan residue in hen's egg-white lysozyme [EC 3.2.1.17] was modified by ozone in an aqueous solution. One of the six tryptophan residues in the enzyme was oxidized to N'-formylkynurenine with concomitant loss of the enzymatic activity. Physicochemical studies of this modified enzyme (OL-I) revealed that the ozonization of lysozyme in aqueous media resulted in little change of the gross molecular conformation. It was deduced that the modified tryptophan residue in OL-I was possibly located in position 62 (or 63) of the protein.
D000596:Amino Acids / Q000032:analysis; D005561:Formates; D007737:Kynurenine; D008837:Micrococcus / Q000187:drug effects; D009113:Muramidase / Q000378:metabolism* / Q000494:pharmacology; D010084:Oxidation-Reduction; D010126:Ozone; D013057:Spectrum Analysis; D014357:Trypsin; D014364:Tryptophan
D000596:Amino Acids; D005561:Formates; D007737:Kynurenine; D010126:Ozone; D014364:Tryptophan; D009113:Muramidase; D014357:Trypsin