Functional characterization of the cyclomarin/cyclomarazine prenyltransferase CymD directs the biosynthesis of unnatural cyclic peptides.
In vitro and in vivo characterization of the cyclomarin/cyclomarazine prenyltransferase CymD revealed its ability to prenylate tryptophan prior to incorporation into both cyclic peptides by the nonribosomal peptide synthetase CymA. This knowledge was utilized to bioengineer novel derivatives of these marine bacterial natural products by providing synthetic N-alkyl tryptophans to a prenyltransferase-deficient mutant of Salinispora arenicola CNS-205.
Schultz
Andrew W
AW
Center for Marine Biotechnology and Biomedicine, Scripps Institution of Oceanography, University of California at San Diego, La Jolla, California 92093-0204, USA.
Lewis
Chad A
CA
Luzung
Michael R
MR
Baran
Phil S
PS
Moore
Bradley S
BS
D039903:Actinobacteria / Q000201:enzymology*; D057005:Bioengineering; D004122:Dimethylallyltranstransferase / Q000172:deficiency / Q000378:metabolism*; D008386:Marine Biology; D015394:Molecular Structure; D010453:Peptide Synthases; D010456:Peptides, Cyclic / Q000096:biosynthesis* / Q000737:chemistry / Q000378:metabolism; D014364:Tryptophan / Q000031:analogs & derivatives* / Q000096:biosynthesis* / Q000737:chemistry
D010456:Peptides, Cyclic; D014364:Tryptophan; D004122:Dimethylallyltranstransferase; D010453:Peptide Synthases; C026269:2,3-dihydroxybenzoate - serine ligase