Change in α-ketoglutarate dehydrogenase cooperative properties due to dihydrolipoate and NADH
Reducing 2 SH-groups of KGD by dihydrolipoate leads to cooperativity in substrate binding. Cooperative properties of KGD in the KGD complex are modulated by NADH. Physiological significance of these observations is discussed.
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| Published in | FEBS letters Vol. 269; no. 1; pp. 252 - 254 |
|---|---|
| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
Amsterdam
Elsevier B.V
20.08.1990
Elsevier |
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| Abstract | Reducing 2 SH-groups of KGD by dihydrolipoate leads to cooperativity in substrate binding. Cooperative properties of KGD in the KGD complex are modulated by NADH. Physiological significance of these observations is discussed. |
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| AbstractList | Reducing 2 SH-groups of KGD by dihydrolipoate leads to cooperativity in substrate binding. Cooperative properties of KGD in the KGD complex are modulated by NADH. Physiological significance of these observations is discussed. Reducing 2 SH-groups of alpha -ketoglutarate dehydrogenase (KGD) by dihydrolipoate leads to cooperativity in substrate binding. Cooperative properties of KGD in the KGD complex are modulated by NADH. Physiological significance of these observations is discussed. |
| Author | Buneeva, O.A. Gomazkova, V.S. Bunik, V.I. |
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| Cites_doi | 10.1016/S0021-9258(18)51823-8 10.1146/annurev.bi.54.070185.001513 10.1016/0006-3002(60)91280-4 10.1016/0076-6879(84)07022-1 |
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| Keywords | NADH KG, α-ketoglutarate KGD, α-ketoglutarate dehydrogenase Dihydrolipoate α-Ketoglutarate dehydrogenase Cooperativity DTNB, 5,5'-dithio-bis-(2-nitrobenzoic) acid CoA, coenzyme A DEP, diethyl pyrocarbonate DTT, dithiothreitol TPP, thiamine pyrophosphate Ligand binding Lipoic acid Vertebrata Regulation(control) Enzymatic activity Muscle Oxoglutarate dehydrogenase Aves Derived product |
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| References | Gomazkova, Stafeeva, Laufer, Severin (BIB7) 1981; 259 Severin, Gomazkova, Krasovskaja, Stafeeva (BIB6) 1978; 43 Gomazkova, Kologrivova, Severin (BIB5) 1985; 10 Bunik, Gomazkova (BIB3) 1985; 50 Massey (BIB11) 1960; 38 Suzuki, Reed (BIB9) 1963; 238 Severin, Gomazkova, Krasovskaja (BIB1) 1974; 218 Gilbert (BIB12) 1984; 107 Ziegler (BIB13) 1985; 54 Bunik, Buneeva, Lvova, Gomazkova (BIB4) 1989; 18 Bunik, Buneeva, Gomazkova (BIB8) 1990 Gomazkova, Bunik, Buneeva (BIB2) 1987; 52 Severin, Gomazkova (BIB10) 1971; 36 1987; 52 1990 1978; 43 1984; 107 1960; 38 1963; 238 1971; 36 1974; 218 1981; 259 1985; 50 1985; 10 1985; 54 1989; 18 Bunik V.I. (e_1_2_1_5_1) 1989; 18 Severin S.E. (e_1_2_1_2_1) 1974; 218 Gomazkova V.S. (e_1_2_1_6_1) 1985; 10 Severin S.E. (e_1_2_1_11_1) 1971; 36 Severin S.E. (e_1_2_1_7_1) 1978; 43 e_1_2_1_12_1 Bunik V.I. (e_1_2_1_9_1) 1990 e_1_2_1_13_1 e_1_2_1_10_1 Bunik V.I. (e_1_2_1_4_1) 1985; 50 e_1_2_1_14_1 Gomazkova V.S. (e_1_2_1_3_1) 1987; 52 Gomazkova V.S. (e_1_2_1_8_1) 1981; 259 |
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| Snippet | Reducing 2 SH-groups of KGD by dihydrolipoate leads to cooperativity in substrate binding. Cooperative properties of KGD in the KGD complex are modulated by... Reducing 2 SH‐groups of KGD by dihydrolipoate leads to cooperativity in substrate binding. Cooperative properties of KGD in the KGD complex are modulated by... Reducing 2 SH-groups of alpha -ketoglutarate dehydrogenase (KGD) by dihydrolipoate leads to cooperativity in substrate binding. Cooperative properties of KGD... |
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| SubjectTerms | Allosteric Regulation Analytical, structural and metabolic biochemistry Animals Biological and medical sciences CoA, coenzyme A Columbidae Cooperativity DEP, diethyl pyrocarbonate Diethyl Pyrocarbonate - pharmacology Dihydrolipoate DTNB, 5,5'-dithio-bis-(2-nitrobenzoic) acid DTT, dithiothreitol Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Ketoglutarate Dehydrogenase Complex - metabolism Ketone Oxidoreductases - metabolism KG, α-ketoglutarate KGD, α-ketoglutarate dehydrogenase Macromolecular Substances Muscles - enzymology NAD - metabolism NADH Oxidation-Reduction Oxidoreductases Protein Conformation Sulfhydryl Compounds Thioctic Acid - analogs & derivatives Thioctic Acid - metabolism TPP, thiamine pyrophosphate α-Ketoglutarate dehydrogenase |
| Title | Change in α-ketoglutarate dehydrogenase cooperative properties due to dihydrolipoate and NADH |
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