EC - Tetracycline polyketide synthase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature


Accepted name:
tetracycline polyketide synthase
Systematic name:
malonyl-CoA:malonamoyl-[OxyC acyl-carrier protein] malonyltransferase



The synthesis, in the bacterium Streptomyces rimosus of the tetracycline antibiotics core skeleton requires a minimal polyketide synthase (PKS) consisting of a ketosynthase (KS), a chain length factor (CLF), and an acyl-carrier protein (ACP). Initiation involves an amide-containing starter unit that becomes the C-2 amide that is present in the tetracycline compounds. Following the initiation, the PKS catalyses the iterative condensation of 8 malonyl-CoA molecules to yield the polyketide backbone of tetracycline. Throughout the proccess, the nascent chain is attached to the OxyC acyl-carrier protein.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB


  1. Thomas, R. and Williams, D.J.
    Oxytetracycline biosynthesis: origin of the carboxamide substituent.
    J. Chem. Soc., Chem. Commun. 677-679 (1983).
  2. Zhang, W., Ames, B. D., Tsai, S. C., Tang, Y.
    Engineered biosynthesis of a novel amidated polyketide, using the malonamyl-specific initiation module from the oxytetracycline polyketide synthase.
    Appl. Environ. Microbiol. 72 : 2573-2580 (2006). [PMID: 16597959]
  3. Yu, L., Cao, N., Wang, L., Xiao, C., Guo, M., Chu, J., Zhuang, Y., Zhang, S.
    Oxytetracycline biosynthesis improvement in Streptomyces rimosus following duplication of minimal PKS genes.
    Enzyme Microb. Technol. 50 : 318-324 (2012). [PMID: 22500899]

[EC created 2016]