The reaction between lentil (Lens culinaris) seedling amine oxidase and its chromogenic substrate, p-dimethylaminomethylbenzylamine, has been studied by the stopped-flow technique. Upon being mixed with substrate in the absence of oxygen, the enzyme is bleached in a complex kinetic process. A yellow intermediate absorbing at 464 nm and the first product (aldehyde) are formed in subsequent steps. When oxygenated buffer is mixed with substrate-reduced amine oxidase, the 496 nm absorption of the oxidized enzyme is very rapidly restored in a second-order process (k = 2.5 X 10(7) M-1 X S-1). This reaction is appreciable even at very low oxygen concentration, in keeping with the fairly low Km for O2 measured by steady-state kinetics.
Transient kinetics of copper-containing lentil (Lens culinaris) seedling amine oxidase / Bellelli, Andrea; Brunori, Maurizio; Finazzi Agró, A; Floris, G; Giartosio, Anna; Rinaldi, A.. - In: BIOCHEMICAL JOURNAL. - ISSN 0264-6021. - STAMPA. - 232:(1985), pp. 923-926.
Transient kinetics of copper-containing lentil (Lens culinaris) seedling amine oxidase.
BELLELLI, Andrea;BRUNORI, Maurizio;GIARTOSIO, Anna;
1985
Abstract
The reaction between lentil (Lens culinaris) seedling amine oxidase and its chromogenic substrate, p-dimethylaminomethylbenzylamine, has been studied by the stopped-flow technique. Upon being mixed with substrate in the absence of oxygen, the enzyme is bleached in a complex kinetic process. A yellow intermediate absorbing at 464 nm and the first product (aldehyde) are formed in subsequent steps. When oxygenated buffer is mixed with substrate-reduced amine oxidase, the 496 nm absorption of the oxidized enzyme is very rapidly restored in a second-order process (k = 2.5 X 10(7) M-1 X S-1). This reaction is appreciable even at very low oxygen concentration, in keeping with the fairly low Km for O2 measured by steady-state kinetics.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.