Christeller J T, Laing W A
Biochem J. 1979 Dec 1;183(3):747-50. doi: 10.1042/bj1830747.
The Michaelis constants of soya-bean ribulose bisphosphate carboxylase for CO2 in the carboxylation reaction and for O2 in the oxygenation reaction depend on the nature of the bivalent cation present. In the presence of Mg2+ the Km for bicarbonate is 2.48 mM, and the Km for O2 is 37% (gas-phase concentration). With Mn2+ the values decrease to 0.85 mM and 1.7% respectively. For the carboxylation reaction Vmax. was 1.7 mumol/min per mg of protein with Mg2+ but only 0.29 mumol/min per mg of protein with Mn2+. For the oxygenation reaction, Vmax. values were 0.61 and 0.29 mumol/min per mg of protein respectively with Mg2+ and Mn2+.
大豆核酮糖二磷酸羧化酶在羧化反应中对二氧化碳以及在加氧反应中对氧气的米氏常数取决于所存在的二价阳离子的性质。在镁离子存在的情况下，碳酸氢盐的米氏常数为2.48毫摩尔，氧气的米氏常数为37%（气相浓度）。在锰离子存在时，这些值分别降至0.85毫摩尔和1.7%。对于羧化反应，镁离子存在时每毫克蛋白质的最大反应速率为1.7微摩尔/分钟，但锰离子存在时每毫克蛋白质仅为0.29微摩尔/分钟。对于加氧反应，镁离子和锰离子存在时每毫克蛋白质的最大反应速率值分别为0.61和0.29微摩尔/分钟。
