The glyoxysomal 3-ketoacyl-CoA thiolase precursor from Brassica napus has enzymatic activity when synthesized in Escherichia coli

Christian Gammelgaard Olesen, Karl Kristian Thomsen, Ib Svendsen, Anders Brandt

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

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.
Original languageEnglish
JournalF E B S Letters
Volume412
Issue number1
Pages (from-to)138-140
ISSN0014-5793
DOIs
Publication statusPublished - 1997
Externally publishedYes

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