The NADP+ - dependent isocitrate dehydrogenase (IDH) from Bacilluslicheniformis was partially purified using ammonium sulphate fractionation andgel filtration on Sephadex G-200 column. The enzyme preparation had specificactivity of 1.52 U mg ’. The temperature optimum for the IDH activity was about59°C. The Arrthenius activation energy was determined to be 65.3 kj/mol below47°C, and 18.3 kJ/mol above this temperature. The IDH activity at 65°C wasmuch protected by isocitrate and magnesium, but no NADP+. Manganese ionswere more efficient activators ofthe enzyme than Mg^+. Calcium ions rather inhibited the IDH. The Km values for DL-isocitrate and NADP+ in phosphate buffer(pH 7.4) at 20°C were 85.5 and 4.9 pM, respectively: at 58°C the correspondingvalues were 181.5 and 69.3 pM.
Operational Program Digital Poland, 2014-2020, Measure 2.3: Digital accessibility and usefulness of public sector information; funds from the European Regional Development Fund and national co-financing from the state budget.
Oct 2, 2020
Sep 14, 2020
|Warunki termostabilności i charakterystyka katalityczna dehydrogenazy izocytrynianowej z Bacillus licheniformis||Oct 2, 2020|
Zabielski, Piotr Strumiło, Sławomir Święcicka, Izabela
Ziółkowski, Piotr Babula- Skowrońska, Danuta Kaczmarek, Małgorzata Cieśla, Agata Sadowski, Jan
Nowak, Jacek K.