[The role of the tryptophan-62 residue in the structure and function of lysozyme].
The thermostability and thermodinamics of formation of the enzyme-substrate complex of two oxidation products of chicken egg lysozyme with the tryptophane-62 residue modified to N'-formylkinurenine (with 2.5% activity) and kinurenine (with 27.5% activity) have been studied. In thermostability and pH effect on the substrate binding the lysozyme oxidation products do not differ from native lysozyme. The data obtained and thermodynamical characteristics of the enzyme-substrate complex formation suggest that the chemical nature of the 62 residue does not significantly affect the  conformational properties of lysozyme, however, having a strongly pronounced effect on the binding of substrate and hence the total enzyme activity.
D055598:Chemical Phenomena; D002621:Chemistry; D004355:Drug Stability; D004531:Eggs; D006863:Hydrogen-Ion Concentration; D007737:Kynurenine; D009113:Muramidase / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D013816:Thermodynamics; D014364:Tryptophan / Q000378:metabolism
D007737:Kynurenine; D014364:Tryptophan; D009113:Muramidase
O roli ostatka triptofana-62 v strukture i funktsii lizotsima