Abstract:
:A cDNA encoding a novel plant type III polyketide synthase (PKS) was cloned from rhubarb (Rheum palmatum). A recombinant enzyme expressed in Escherichia coli accepted acetyl-CoA as a starter, carried out six successive condensations with malonyl-CoA and subsequent cyclization to yield an aromatic heptaketide, aloesone. The enzyme shares 60% amino acid sequence identity with chalcone synthases (CHSs), and maintains almost identical CoA binding site and catalytic residues conserved in the CHS superfamily enzymes. Further, homology modeling predicted that the 43-kDa protein has the same overall fold as CHS. This provides new insights into the catalytic functions of type III PKSs, and suggests further involvement in the biosynthesis of plant polyketides.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Abe I,Utsumi Y,Oguro S,Noguchi Hdoi
10.1016/S0014-5793(04)00230-3keywords:
subject
Has Abstractpub_date
2004-03-26 00:00:00pages
171-6issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579304002303journal_volume
562pub_type
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