Tetracenomycin synthase

Figure 12.5 A. Comparison of the CHS monomer (left) and P-ketoacyl synthase monomer (right). The structurally conserved secondary structure of each monomer s upper domain is colored in blue (a-helix) and gold (P-strand). Portions of each protein monomer forming the dimer interface are colored purple. The side-chains of the catalytic residues of CHS (Cysl64, His303, Asn336) and P-ketoacyl synthase (Cysl63, His303, His340) are shown. B. Sequence conservation of the catalytic residues of CHS, 2-PS, p-ketoacyl synthase (FAS II), and the ketosynthase modules of 6-deoxyerythronolide B synthase (DEBS), actinorhodin synthase (ActI) and tetracenomycin synthase (TcmK). The catalytic residues are in red.

A. Actinorhodin, Tetracenomycin, Doxorubicin, and Other Bacterial Aromatic Polyketide Synthases... 

W Bao, E Wendt-Pienkowski, CR Hutchinson. Reconstitution of the iterative type II polyketide synthase for tetracenomycin F2 biosynthesis. Biochemistry 37 8132-8138, 1998. 

HC Gramajo, J White, CR Hutchinson, MJ Bibb. Overproduction and localization of components of the polyketide synthase of Streptomyces glaucescens involved in the production ofthe antibiotic tetracenomycin C. JBacteriol 173 6475-6483,1991. 

B Shen, RG Summers, H Gramajo, MJ Bibb, CR Hutchinson. Purification and characterization of the acyl carrier protein of the Streptomyces glaucescens tetracenomycin C polyketide synthase. JBacteriol 174 3818-3821, 1992. 

Fig. 5. In vitro synthesis of tetracenomycins and their shunt metabolites from acetyl CoA and malonyl CoA by the TcmKLM polyketide synthase complex, the TcmJ, TcmN, and Tcml cyclases, and the TcmH monoxygenase...

---