Zabielski, Piotr ; Strumiło, Sławomir ; Święcicka, Izabela
Committee on Biotechnology PAS ; Institute of Bioorganic Chemistry PAS
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.
Biotechnologia, vol.54, 3 (2001)-.
0860-7796 ; oai:rcin.org.pl:138907 ; IChB B-50
Library of Institute of Bioorganic Chemistry PAS
Creative Commons Attribution BY-SA 4.0 license
Institute of Bioorganic Chemistry of the Polish Academy of Science
Institute of Bioorganic Chemistry of the Polish Academy of Science
Oct 2, 2020
Sep 14, 2020
302
https://rcin.org.pl/publication/174189
Edition name | Date |
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Warunki termostabilności i charakterystyka katalityczna dehydrogenazy izocytrynianowej z Bacillus licheniformis | Oct 2, 2020 |
Borkowska, Bożenna
Ziółkowski, Piotr Babula- Skowrońska, Danuta Kaczmarek, Małgorzata Cieśla, Agata Sadowski, Jan