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On January 31st, scientific reports, an international academic journal, published online the latest research results of the National Key Laboratory of Molecular Biology of the Institute of Molecular Cell Science of the Chinese Academy of Sciences/Shanghai Institute of Biochemistry and Cell Biology, and the Ding Jianping Research Group of the National Protein Science Center (Shanghai): The b and g subunits play distinct functions in the a2bg heterotetramer of human NAD-dependentocitrate.
the study revealed that b and g subkeys of the human-sourced NAD-dependent iso-citric acid dehydrogenase (NAD-IDH) perform different biological functions in the whole enzyme.
IDH is a family of enzymes widely found in organisms that use NADP or NAD as coenzyme catalytic isocitrate (ISTOCITrate, ICT) oxidation to produce a-ketone diacid.
Theocle organism has two IDHs of NADP and NAD dependence, where NADP-IDH is found in cell pulp, mitochondrials and peroxidases, and has been found to play an important role mainly in cell antioxidant damage, detoxification of reactive oxygen free agents, and fat and cholesterol synthesis;
Jianping Research Group has long been engaged in the structure and function of the thermobon isochloric acid dehydrogenase, and has determined the human plasma NADP-IDH and yeast mitochondrial NADP-IDH and coenzyme, bottom the crystal structure of complexes such as metal ions and products, and carried out bio-chemical and functional studies to reveal the biological function of NADP-IDH and its molecular basis leading to disease (J.Biol.Chem., 2004; Protein Sci., 2008; Cell Res., 2010).
Mammal NAD-IDH is composed of a, b, and g sub-base in a ratio of 2:1:1, where a sub-base is catalytic sub-base, involved in the binding of substrates, cofactors, metal ions, while b and g sub-base are considered to regulate sub-base, may have the ability to combine regulatory factors.
previous research has found that mammalian NAD-IDH can be regulated by factors such as citric acid CIT and ADP, thus changing its affinity for the substrate ISCIT, but without affecting the maximum reaction rate.
a and b sub-base or a and g sub-base can form a basic structural unit, and have a certain vitality, ab and ag heterogeneous binary assembly into octa-polyenzyme function, but b and g two regulating sub-base in structure and function differences, and their mechanism for other structural adjustment is not clear.
Ma Tengfei, an assistant researcher in the Ding Jianping Research Group, and others systematically studied the enzymatic properties of human-sourced NAD-IDH whole enzymes and ab and ag heterogeneous binary regulatory factors before and after activation.
data show that both ab and ag heterogeneous binary have catalytic vitality, but show different enzymatic properties.
ag heterogeneous binary represents enzyme dynamics parameters similar to that of whole enzymes, which can be regulated by the structure of CIT and ADP, and can be activated by low-concentration ATP and inhibited by high-concentration ATP.
, ab heterogeneous binary can not be regulated by CIT and ADP structure, and can only be inhibited by ATP.
experimental researchers using mutants also found that ab and ag heterogeneous binary contributions to the vitality of the whole enzyme were comparable before and after the activation of the regulatory factor, and could be regulated by the structure of CIT and ADP by g sub-base rather than b sub-base.
these results illustrate for the first time the functional differences between b and g-regulating sub-base, i.e. g sub-base in human-source NAD-IDH whole enzyme, while b sub-base plays a structural function mainly in whole enzyme assembly.
the research work has been supported by the National Natural Science Foundation of China, the Ministry of Science and Technology and the Chinese Academy of Sciences.
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