FEBS Letters | |
Cloning and expression in yeast of a higher plant chorismate mutase Molecular cloning, sequencing of the cDNA and characterization of the Arabidopsis thaliana enzyme expressed in yeast | |
Schmid, Jürg1  Amrhein, Nikolaus1  Eberhard, Jenny1  Raesecke, Hanns-R.1  | |
[1] Institute of Plant Sciences, Swiss Federal Institute of Technology, Universitätstrasse 2, CH-8092 Zürich, Switzerland | |
关键词: Shikimate pathway; Chorismate mutase; Arabidopsis thaliana; | |
DOI : 10.1016/0014-5793(93)81718-F | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Chorismate mutase (EC 5.4.99.5) catalyzes the first step in the branch of the shikimate pathway which leads to the aromatic amino acids, phenylalanine and tyrosine. We have isolated a cDNA for this enzyme from the higher plant, Arabidopsis thaliana, by complementing a yeast strain (aro7) with a cDNA library from A. thaliana. This is the first chorismate mutase cDNA isolated from a plant. It encodes a protein of 334 amino acids. The identity of the deduced amino acid sequence is 41% to the chorismate mutase sequence from Saccharomyces cerevisiae. The N-terminal portion of the deduced amino acid sequence has no homology to the S. cerevisiae sequence but resembles known plastid-specific transit peptides. The A. thaliana chorismate mutase expressed in yeast revealed allosteric control by the three aromatic amino acids, as previously described for plastidic chorismate mutase isozymes.
【 授权许可】
Unknown
【 预 览 】
Files | Size | Format | View |
---|---|---|---|
RO201912020298728ZK.pdf | 405KB | download |