THE STRUCTURE OF CAT MUSCLE PYRUVATE-KINASE
THE STRUCTURE OF CAT MUSCLE PYRUVATE-KINASE
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DOI：
10.1002/j.1460-2075.1986.tb04236.x
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发表时间：
1986-03-01
期刊：
影响因子：
11.4
通讯作者：
SCHMITT, W
中科院分区：
文献类型：
--
作者：
MUIRHEAD, H;CLAYDEN, DA;SCHMITT, W
测定了猫肌丙酮酸激酶的全氨基酸序列，并与2.6ANG.分辨率电子密度图活性位点区域中的残基在猫肌肉、鸡肌肉、大鼠肝脏和酵母酶中高度保守。酶结合的镁，这是必不可少的活动，相互作用的侧链谷氨酸-271和两个主要的羰基。赖氨酸-269可能是负责丙酮酸和烯醇丙酮酸相互转化的酸/碱催化剂。一个可能的结合位点的必要的单价阳离子的建议。
The complete amino acid sequence of cat muscle pyruvate kinase has been determined and fitted to the 2.6 .ANG. resolution electron density map. Residues in the active site region are highly conserved in the cat muscle, chicken muscle, rat liver and yeast enzymes. The enzyme-bound magnesium, which is essential for activity, interacts with the side chain of glutamate-271 and with two main carbonyl groups. Lysine-269 is the probable acid/base catalyst responsible for the interconversion of pyruvate and enolpyruvate. A possible binding site for the essential monovalent cation is proposed.