FEBS Letters | |
The glyoxysomal 3‐ketoacyl‐CoA thiolase precursor from Brassica napus has enzymatic activity when synthesized in Escherichia coli | |
Brandt, Anders2  Svendsen, Ib1  Thomsen, Karl Kristian2  Olesen, Christian2  | |
[1] Department of Chemistry, Carlsberg Laboratory, Gamle Carlsbergvej 10, DK-2500 Copenhagen Valby, Denmark;Department of Physiology, Carlsberg Laboratory, Gamle Carlsbergvej 10, DK-2500 Copenhagen Valby, Denmark | |
关键词: Expression; Microbody; Presequence; | |
DOI : 10.1016/S0014-5793(97)00766-7 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Glyoxysomal 3-ketoacyl-CoA thiolase is the last enzyme in the β-oxidation of fatty acids in plant glyoxysomes. A full-length cDNA of the glyoxysomal 3-ketoacyl-CoA thiolase from Brassica napus and a truncated version, lacking the N-terminal targeting signal were cloned in a T7 promoter-based vector. Both recombinant proteins were expressed in Escherichia coli and activity was measured. Full-length and truncated 3-ketoacyl-CoA thiolase have comparable activity in E. coli. Moreover, full-length 3-ketoacyl-CoA thiolase was purified from E. coli and N-terminal sequencing of the protein confirmed that the precursor form indeed is enzymatically active.
【 授权许可】
Unknown
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