猫肌肉丙酮酸激酶的结构。
The structure of cat muscle pyruvate kinase.
作者信息
Muirhead H, Clayden D A, Barford D, Lorimer C G, Fothergill-Gilmore L A, Schiltz E, Schmitt W
出版信息
EMBO J. 1986 Mar;5(3):475-81. doi: 10.1002/j.1460-2075.1986.tb04236.x.
Abstract
The complete amino acid sequence of cat muscle pyruvate kinase has been determined and fitted to the 2.6 A 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.
摘要
猫肌肉丙酮酸激酶的完整氨基酸序列已被确定，并与分辨率为2.6埃的电子密度图相匹配。活性位点区域的残基在猫肌肉、鸡肌肉、大鼠肝脏和酵母酶中高度保守。对活性至关重要的酶结合镁与谷氨酸-271的侧链以及两个主要羰基相互作用。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。提出了必需单价阳离子的一个可能结合位点。
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The M1 and M2 subunits of rat pyruvate kinase are encoded by different messenger RNAs.大鼠丙酮酸激酶的M1和M2亚基由不同的信使核糖核酸编码。
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