Isocitrate dehydrogenase of Tetrahymena pyriformis

作者: Pilar Vidal , Alberto Machado

DOI: 10.1007/BF01730835

关键词: BiochemistryNAD+ kinaseChemistryDivalentEnzymeIsocitrate dehydrogenaseClinical chemistryPhysiological significanceTetrahymena pyriformisIDH1Clinical biochemistryCell biologyMolecular biologyGeneral Medicine

摘要: We have studied the isocitrate dehydrogenase ofTetrahymena pyriformis. This enzyme is able to utilize both NAD and NADP, but kinetic studies suggest that enzymatic activity with not of physiological significance.

参考文章(37)
Guünther Siebert, M. Carsiotis, G.W.E. Plaut, The enzymatic properties of isocitric dehydrogenase Journal of Biological Chemistry. ,vol. 226, pp. 977- 991 ,(1957) , 10.1016/S0021-9258(18)70883-1
Earl Shrago, Wolfgang Brech, Karen Templeton, Glyconeogenesis in Tetrahymena pyriformis RELATIONSHIP OF ENZYME ADAPTATION TO THE CARBON PATHWAY Journal of Biological Chemistry. ,vol. 242, pp. 4060- 4066 ,(1967) , 10.1016/S0021-9258(18)95778-9
Jerry S. Hubbard, Alan B. Miller, Purification and Reversible Inactivation of the Isocitrate Dehydrogenase from an Obligate Halophile Journal of Bacteriology. ,vol. 99, pp. 161- 168 ,(1969) , 10.1128/JB.99.1.161-168.1969