Quaternary structure of pigeon liver malic enzyme
- 17 December 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 277 (1-2) , 175-179
- https://doi.org/10.1016/0014-5793(90)80837-9
Abstract
Pigeon liver malic enzyme (EC 1.1.1.40) has a double dimer quaternary structure. The NADP+ analogs, aminopyridine adenine dinucleotide phosphate and nicotinamide-1.N 6-ethenoadenosine dinucleotide phosphate, bind to the enzyme anti-cooperatively. In the presence of non-cooperative competing ligand NADP+ the binding parameter Hill coefficients of these analogues changed very little. Binding of L-malate with enzyme-AADP+ complex first enhanced then reduced the nucleotide fluorescence. Two L-malate binding sites, with K d values of 23–30 and 270–400 μM, respectively, for the tight and weak binding sites were postulated. A hybrid model between the sequential and pre-existing asymmetrical models was proposed for the pigeon liver malic enzyme.Keywords
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