荧光假单胞菌对羟基苯甲酸羟化酶的一级结构
Primary structure of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens.
作者信息
Weijer W J, Hofsteenge J, Vereijken J M, Jekel P A, Beintema J J
出版信息
Biochim Biophys Acta. 1982 Jun 4;704(2):385-8. doi: 10.1016/0167-4838(82)90170-4.
The amino acid sequence of the p-hydroxybenzoate hydroxylase (4-hydroxybenzoate,NADPH:oxygen oxidoreductase (3-hydroxylating), EC 1.14.13.2) monomer from Pseudomonas fluorescens has been determined. The sequence was elucidated by a combination of the results from an X-ray crystallographic study at 0.25 nm resolution (Wierenga, R.K., de Jong, R.J., Kalk, K.H., Hol, W.G.J. and Drenth, J. (1979) J. Mol. Biol. 131, 55-73) and from protein sequence analysis. The polypeptide chain of the monomer contains 394 amino acids and has a molecular weight of 44 299.
已确定荧光假单胞菌对羟基苯甲酸羟化酶（4-羟基苯甲酸，NADPH：氧氧化还原酶（3-羟基化），EC 1.14.13.2）单体的氨基酸序列。该序列是通过结合0.25纳米分辨率的X射线晶体学研究结果（维伦加，R.K.，德容，R.J.，卡尔克，K.H.，霍尔，W.G.J.和德伦特，J.（1979年）《分子生物学杂志》131卷，55 - 73页）和蛋白质序列分析得出的。单体的多肽链包含394个氨基酸，分子量为44299。
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