PHOSPHOENOLPYRUVATE-DEPENDENT PHOSPHOTRANSFERASE SYSTEM OF STAPHYLOCOCCUS-AUREUS .1. AMINO-ACID-SEQUENCE OF PHOSPHOCARRIER PROTEIN-HPR
PHOSPHOENOLPYRUVATE-DEPENDENT PHOSPHOTRANSFERASE SYSTEM OF STAPHYLOCOCCUS-AUREUS .1. AMINO-ACID-SEQUENCE OF PHOSPHOCARRIER PROTEIN-HPR
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DOI：
10.1111/j.1432-1033.1977.tb11527.x
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发表时间：
1977-01-01
期刊：
影响因子：
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通讯作者：
HENGSTENBERG, W
中科院分区：
文献类型：
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作者：
BEYREUTHER, K;RAUFUSS, H;HENGSTENBERG, W
来自金黄色葡萄球菌的磷酸烯醇丙酮酸依赖性磷酸转移酶系统的含组氨酸的磷酸载体蛋白HPr的一级结构通过自动Edman降解测定。完整的序列是通过在 Edman 液相测序仪中通过自动 Edman 降解对蛋白质进行直接分析以及通过在固相测序仪中通过自动 Edman 降解获得的胰蛋白酶 [EC 3.4.21.4]、热解 [EC 3.4.24.4] 和 CNBr 肽的序列推导出来的。氨基酸序列为Met-Glu-Gln-Asn-Ser-Tyr-Val-Ile-Ile-Asp-Glu-Thr-Gly-Ile-His-Ala-Arg-Pro-Ala-Thr-Met-Leu-Val-Gln-Thr-Ala-Ser-Lys-Phe-Asp-Ser-Ile-Asp-Gln-Gly- Gly-Tyr-Asp-Ser-Met-Gln-Leu-Lys-Ser-Leu-Gly-Val-Gly-Lys-Asp-Glu-Glu-Ile-Thr-Ile-Tyr-Ser-Ala-Asp-Lys-Lys-Glu-Gly-Leu-Thr-Lys-Met-Ser-Ile-Val。 70 个残基对应于 7685 的 MW。参与该蛋白质磷酸转移反应的 1 个组氨酸位于位置 15，作为序列区域的一部分，该区域没有可预测的二级结构。该蛋白质可能属于活性中心位于突起而不是裂缝上的雄性蛋白质组。
The primary structure of the histidine-containing phosphocarrier protein HPr of the phosphoenolpyruvate-dependent phosphotransferase system from S. aureus was determined by automated Edman degradation. The complete sequence was deduced from the direct analysis of the protein by automated Edman degradation in a liquid-phase sequencer of Edman and from the sequence of tryptic [EC 3.4.21.4], thermolytic [EC 3.4.24.4] and CNBr peptides as obtained by automated Edman degradation in a solid-phase sequencer. The amino-acid sequence was Met-Glu-Gln-Asn-Ser-Tyr-Val-Ile-Ile-Asp-Glu-Thr-Gly-Ile-His-Ala-Arg-Pro-Ala-Thr-Met-Leu-Val-Gln-Thr-Ala-Ser-Lys-Phe-Asp-Ser-Ile-Asp-Gln-Gly-Gly-Tyr-Asp-Ser-Met-Gln-Leu-Lys-Ser-Leu-Gly-Val-Gly-Lys-Asp-Glu-Glu-Ile-Thr-Ile-Tyr-Ser-Ala-Asp-Lys-Lys-Glu-Gly-Leu-Thr-Lys-Met-Ser-Ile-Val. The 70 residues correspond to a MW of 7685. The 1 histidine involved in the phosphotransfer reaction of this protein was at position 15 as part of a region of the sequence which has no predictable secondary structure. This protein probably belongs to the group of male proteins with the active center located on a protrusion rather than a cleft.