*5.2.4 Prenylation*

Prenylagarmide (pag), trunkamide (tru). Aesturamide (lyn) pathways, encodes the prenyltransferase gene, capable of synthesizing prenylated compounds. Prenyltransferase gene present in patellamide, generates non-prenylated patellamide A and C. Trunkamide contains O-prenylated threonine and serine (**Figure 4**(**c**)). Prenylagarmide contains O-prenylated tyrosine. Prenyltransferase from lyn (LynF) and tru (TruF) pathways. Prenyltransferase from lyn (LynF) and tru (TruF) pathways have been characterized biochemically. However, the reverse O-Prenylated tyrosine undergoes spontaneous claisen rearranging and yieding ortho-substituited phenol. LynF prenylates the oxygen atom of tyrosine residue by using dimethylallylpyrophosphate (DMAPP). TruF prenylates serine and threonine residues on the hydroxyl side chain. PatF from the patellamide pathway, it embraces the other prenyltransferase, classic TIM barrel fold. No enzymatic activity was detected, may be due to absence of prenylation in patellamides A and C. PatF essential for the production of patellamide in vivo and consequently responsible for another function in this pathway. Oxidase domain is conserved among PatG homologs and studies put up a prediction that FMN id dependent. Thiazoline oxidase has been related in sequence to the patellamide enzyme. However its action on microcin pathway was a matter of biochemical study. How this enzyme recognizes the substrate remains unclear, as the microns are linear and patellamides are macrocyclase. One homolog of the oxidase domain of PatG was capable of oxidizing both linear and macrocycle thiazoline containing compounds and another homolog has the ability to perform oxidation on a macrocyclic substrate.
