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葡萄糖-6-磷酸脱氢酶。毕赤酵母中该酶一个活性赖氨酸残基的特性揭示了功能重要区段中有限的结构变异。

Glucose-6-phosphate dehydrogenase. Characterization of a reactive lysine residue in the Pichia jadinii enzyme reveals a limited structural variation in a functionally significant segment.

作者信息

Jeffery J, Wood I, Macleod A, Jeffery R, Jörnvall H

机构信息

Department of Biochemistry, University of Aberdeen, Marischal College, Scotland, UK.

出版信息

Biochem Biophys Res Commun. 1989 May 15;160(3):1290-5. doi: 10.1016/s0006-291x(89)80143-3.

Abstract

Glucose-6-phosphate dehydrogenase from the yeast Pichia jadinii has a reactive lysine residue in a segment of amino acid sequence Ile-Asp-His-Tyr-Leu-Gly-Lys*-Glu-Met-Val-Lys. This structure differs from that of other characterized glucose-6-phosphate dehydrogenases, but outside yeasts the segment is invariant in known mammalian, insect and bacterial forms. Thus, limited structural variation is now defined within yeasts for a part of the protein otherwise strictly conserved, and for which stringent structural requirements probably relate to enzymic mechanisms.

摘要

来自季也蒙毕赤酵母的葡萄糖-6-磷酸脱氢酶在一段氨基酸序列Ile-Asp-His-Tyr-Leu-Gly-Lys*-Glu-Met-Val-Lys中有一个活性赖氨酸残基。该结构与其他已鉴定的葡萄糖-6-磷酸脱氢酶不同,但在酵母之外,该片段在已知的哺乳动物、昆虫和细菌形式中是不变的。因此,现在在酵母中定义了该蛋白质一部分的有限结构变异,而该部分蛋白质在其他情况下是严格保守的,并且严格的结构要求可能与酶促机制有关。

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