Kinetic characteristics of L-lysine α- oxidase from Trichoderma cf. aureoviride Rifai VKM F-4268D: Substrate specificity and allosteric effects

摘要: The present work aims to investigate the kinetic characteristics of homodimer enzyme L-lysine α-oxidase from Trichoderma cf. aureoviride Rifai VKM F-4268D, taking into account allosteric effects. was first shown reveal positive cooperativeness, h=2.05±0.15. Using additional opportunities Hill coefficient value Michaelis-Menten constant has been estimated, Km=1.015∙10-5М, indicating high strength substrate binding active site each subunit. High selectivity and absolute L-stereospecificity were shown. inhibition conversion by non-cleavable lysine analogs as well reaction product found out take place. These effects have evaluated only coefficients (%). A more detailed study these complicated because cooperativeness subunits mentioned above. scheme proposed involving parallel-subsequent action two in catalytic act. We think that results obtained will be useful for studying properties other multi-subunit enzymes improve understanding mechanisms their action.