FIGURE 3 | ACV synthetase, a trimodular non-ribosomal peptide synthetase.

From the following article:

Fungal secondary metabolism — from biochemistry to genomics

Nancy P. Keller, Geoffrey Turner & Joan W. Bennett

Nature Reviews Microbiology 3, 937-947 (December 2005)

doi:10.1038/nrmicro1286

Fungal secondary metabolism |[mdash]| from biochemistry to genomics

delta-(L-alpha-aminoadipyl) L-cysteinyl-D-valine (ACV) synthetase catalyses the first committed step in penicillin and cephalosporin biosynthesis. Each amino acid is recognized and activated by the cognate adenylation domain (A), and attached as a thioester to 4'-phosphopantetheine at the peptidyl carrier domain (P). Peptide bonds are formed with the involvement of the condensation domain (C). The final tripeptide, attached to the peptidyl carrier domain of the C-terminal module, is released by the integrated thioesterase domain (TE), with the L-valine isomerized to D-valine. The tripeptide is subsequently cyclized to isopenicillin N.

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