从人类红细胞谷胱甘肽还原酶。NADPH的序列接口的域和域。
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Krauth-Siegel RL Blatterspiel R,萨利赫M, Schiltz E Schirmer RH, Untucht-Grau R
从人类红细胞谷胱甘肽还原酶。NADPH的序列接口的域和域。
121年1月,欧元。1982 (2):259 - 67。
- PubMed ID
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7060551 (在PubMed]
- 文摘
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1。序列分析的NADPH域(残留158 - 293)和接口的域(365 - 478)是基于12 CNBr片段,孤立使用离子交换色谱和纸的方法。与超过15残留碎片是进一步与胰蛋白酶和胰凝乳蛋白酶消化。孤立的肽被自动化固相埃德曼降解测序。所有测序肽被命令和重叠的电脑与一个完整的序列猜电子密度图的蛋白质。对于短CNBr片段,证实了该联合产生的蛋白质片段的序列分析不完整的CNBr乳沟。2。NADPH域,剩余197,参与诱导契合机制,被认定为酪氨酸。NADPH的结构域可能是同源的NAD域lipoamide脱氢酶和时尚领域的几个蛋白质,但不使用域已知chain-fold NADPH在其他蛋白质。3所示。 The paper completes the sequence analysis of glutathione reductase so that the enzyme is now known in atomic detail. The numbering scheme of the chemically determined sequence will be used henceforth in crystallographic studies also. As inferred from the sequence data each of the two identical chains contains 478 amino acid residues, the composition being Cys10, Asp21, Asn17, Thr31, Ser31, Glu29, Gln11, Pro24, Gly43, Ala42, Val44, Met15, Ile29, Leu34, Tyr13, Phe14, Lys34, His16. Arg17, and Trp3. From these data an Mr of 2 x 51 600 was calculated for the FAD-free apoenzyme and an Mr of 2 x 42 400 for the holoenzyme.