Enrichment of enzyme activity on deformylation of 1-NFK-lysozyme.
The formamide linkage of an inactive lysozyme derivative (1-NFK-lysozyme), formed by selective ozonization of tryptophan 62 in hen egg-white lysozyme [EC 3.2.1.17] was hydrolyzed with dilute acid faster in the frozen state at about --10 degrees than at 20 degrees. On hydrolysis of 1-NFK-lysozyme the low lytic activity increased to approximately 80% of that of native lysozyme. It is suggested that the binding ability associated with kynurenine 62 in the lysozyme derivative formed by this hydrolysis may be responsible for increase in enzymatic activity.
D001665:Binding Sites; D002846:Chromatography, Affinity; D004529:Egg White; D005559:Formamides; D007700:Kinetics; D007737:Kynurenine; D009113:Muramidase; D010126:Ozone; D010446:Peptide Fragments / Q000032:analysis; D011485:Protein Binding; D013696:Temperature; D014357:Trypsin; D014364:Tryptophan
D005559:Formamides; D010446:Peptide Fragments; D007737:Kynurenine; D010126:Ozone; D014364:Tryptophan; D009113:Muramidase; D014357:Trypsin