QUATERNARY STRUCTURE OF PIGEON LIVER MALIC ENZYME

被引:13
作者
LEE, HJ [1 ]
CHANG, GG [1 ]
机构
[1] NATL DEF MED CTR,DEPT BIOCHEM,POB 90048,TAIPEI,TAIWAN
关键词
QUATERNARY STRUCTURE; LIGAND BINDING; NADP ANALOG; ASYMMETRIC MODEL; MALIC ENZYME; PIGEON LIVER;
D O I
10.1016/0014-5793(90)80837-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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,N6-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 mu-M, 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.
引用
收藏
页码:175 / 179
页数:5
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