Department of Biotechnology, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.
Extremophiles. 2011 May;15(3):359-64. doi: 10.1007/s00792-011-0367-2. Epub 2011 Apr 2.
A membrane-intrinsic acid pyrophosphatase (ST2226) from Sulfolobus tokodaii, a thermoacidophilic archaeon, is possibly involved in glycoprotein biosynthesis and belongs to the phosphatidic acid phosphatase class 2 superfamily, including both membrane-intrinsic and soluble enzymes with divergent functions ranging from dephosphorylation of undecaprenylpyrophosphate and phospho-monoesters such as glucose-6-phosphate to vanadium-containing chloroperoxidation. ST2226 is an archaeal ortholog of these enzymes sharing a common phosphatase motif. Through site-directed mutagenesis as to each of the conserved residues, the catalytic roles of the latter were deduced, as well as the transmembrane topology with all the conserved residues in close proximity to the outside of the membrane.
一种来自嗜热嗜酸古菌（Sulfolobus tokodaii）的膜内在酸性焦磷酸酶（ST2226）可能参与糖蛋白的生物合成，属于磷酸脂酶类 2 超家族，包括具有不同功能的膜内在和可溶性酶，其功能从去磷酸化十一碳烯焦磷酸和磷酸单酯（如葡萄糖-6-磷酸）到含钒的氯化过氧化物酶不等。ST2226 是这些酶的古菌同源物，它们具有共同的磷酸酶基序。通过对每个保守残基进行定点诱变，推导出了后者的催化作用，以及所有保守残基都靠近膜外的跨膜拓扑结构。
