4 research outputs found
Kinetic characteristics of L-lysine Ξ±- oxidase from Trichoderma cf. aureoviride Rifai VKM F-4268D: Substrate specificity and allosteric effects
The present work aims to investigate the kinetic characteristics of homodimer enzyme L-lysine Ξ±-oxidase from Trichoderma cf. aureoviride Rifai VKM F-4268D, taking into account allosteric effects. The enzyme was first shown to reveal positive cooperativeness, h=2.05Β±0.15. Using additional opportunities of Hill coefficient the value of the MichaelisβMenten constant has been estimated, Km=1.015β10β5Π, indicating high strength of substrate binding to the active site of each subunit. High selectivity and absolute L-stereospecificity of the enzyme were shown. The inhibition of L-lysine conversion by non-cleavable lysine analogs as well as the reaction product was found out to take place. These effects have been evaluated only as the inhibition coefficients (%). A more detailed study of these inhibition effects was complicated because of the cooperativeness of enzyme subunits mentioned above. The kinetic scheme of L-lysine Ξ±-oxidase was proposed involving parallel-subsequent action of each of two subunits in the catalytic act.
We think that the results obtained will be useful for studying the kinetic properties of other multi-subunit enzymes and improve understanding of the mechanisms of their action
Plant proteome. Changes during ageing and under environmental stress conditions
ΠΠ»Π΅ΡΠΎΡΠ½Π°Ρ Π±ΠΈΠΎΠ»ΠΎΠ³ΠΈΡ. ΠΠΎΠ»Π΅ΠΊΡΠ»ΡΡΠ½ΡΠ΅ ΠΈ Π±ΠΈΠΎΡ
ΠΈΠΌΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΎΡΠ½ΠΎΠ²Ρ ΠΊΠ»Π΅ΡΠΎΡΠ½ΡΡ
ΡΡΠ½ΠΊΡΠΈΠΉThe work was supported by Russian Science Foundation (project β17-16-01042)
Plant proteome. Changes during ageing and under environmental stress conditions
ΠΠ»Π΅ΡΠΎΡΠ½Π°Ρ Π±ΠΈΠΎΠ»ΠΎΠ³ΠΈΡ. ΠΠΎΠ»Π΅ΠΊΡΠ»ΡΡΠ½ΡΠ΅ ΠΈ Π±ΠΈΠΎΡ
ΠΈΠΌΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΎΡΠ½ΠΎΠ²Ρ ΠΊΠ»Π΅ΡΠΎΡΠ½ΡΡ
ΡΡΠ½ΠΊΡΠΈΠΉThe work was supported by Russian Science Foundation (project β17-16-01042)