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 language | English |
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Journal | F E B S Letters |
Volume | 412 |
Issue number | 1 |
Pages (from-to) | 138-140 |
ISSN | 0014-5793 |
DOIs | |
Publication status | Published - 1997 |
Externally published | Yes |