Search for: [Abstract = "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."]

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