Amino acid sequence of spinach ferredoxin:NADP+ oxidoreductase.
Amino acid sequence of spinach ferredoxin:NADP+ oxidoreductase.
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DOI：
10.1021/bi00321a046
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发表时间：
1984-12
期刊：
影响因子：
2.9
通讯作者：
P. Karplus;K. Walsh;J. Herriott
中科院分区：
文献类型：
--
作者：
P. Karplus;K. Walsh;J. Herriott
菠菜铁氧还蛋白：NADP+氧化还原酶的氨基酸序列的测定通过使用重叠的肽组，所述肽组通过在异戊酰基或甲硫氨酰基残基处裂解而得到。来自不同制备物的蛋白质在其氨基末端的长度上不同。在最长的形式中，氨基末端被焦谷氨酰基残基封闭，如通过NMR测定的。在半胱氨酸残基132和137之间放置单个二硫键。314个残基序列对应于35 317的分子量。羧基末端的一半序列已被拟合的NADP结合域的电子密度图，揭示了这部分链形成一个典型的核苷酸结合折叠。
The amino acid sequence of spinach ferredoxin: NADP+ oxidoreductase was determined by using overlapping sets of peptides derived by cleavage at arginyl or methionyl residues. The protein from different preparations varied in its length at the amino terminus. In the longest form the amino terminus is blocked with a pyroglutamyl residue, as determined by NMR. A single disulfide bond was placed between cysteine residues 132 and 137. The 314-residue sequence corresponds to a molecular weight of 35 317. The carboxyl-terminal half of the sequence has been fit to the electron density map of the NADP binding domain, revealing that this portion of the chain forms a typical nucleotide binding fold.