Jeffery J, Wood I, Macleod A, Jeffery R, Jörnvall H
Department of Biochemistry, University of Aberdeen, Marischal College, Scotland, UK.
Biochem Biophys Res Commun. 1989 May 15;160(3):1290-5. doi: 10.1016/s0006-291x(89)80143-3.
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.
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。