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Biocatalysts: The Different Classes and Applications for Synthesis of APIs
Published in Peter Grunwald, Pharmaceutical Biocatalysis, 2019
An example of how nature uses the catalytic potential of cytochrome P450 enzymes has been published by Brieke et al. (2015) who investigated the participation of these enzymes in the non-ribosomal peptide synthase (NRPS)-catalyzed biosynthesis of glycopeptide antibiotics such as vancomycin and teicoplanin. The NRPS in its terminal module contains a recruitment domain (a modified condensation domain) for two P450 enzymes (OxyB and OxyA) that are responsible for the sequential cyclization of the peptide precursor attached to the adjacent peptide carrier protein; this occurs prior to the final decoration of the molecules with other—mainly sugar—moieties and is to a high degree essential for their antibacterial activity.
Toxicity and applications of surfactin for health and environmental biotechnology
Published in Journal of Toxicology and Environmental Health, Part B, 2018
Vanessa Santana Vieira Santos, Edgar Silveira, Boscolli Barbosa Pereira
Surfactin is synthesized nonribosomally by the multi-modular enzyme complex termed nonribosome peptide synthases (NRPS), which recognize, activate, modify, and link amino acid intermediates to generate the peptide (Inés and Dhouha 2015), assembling the molecule through successive additions of amino acids (Chooi and Tang 2010). The fatty acyl chain is the first structure incorporated into the peptidyl backbone via a mechanism known as lipoinitiation (Chooi and Tang 2010). The NRPS enzymes present a modular structure composed of multiple catalytic domains joined as a multi-domain protein (Mitchell et al. 2012). The structure possesses three core domains that include (a) an upstream adenylation domain, (b) an upstream condensation domain, responsible for the formation of the peptide bond, and (c) a terminal thioesterase domain (TE). Initially, amino acids and peptide substrates are adenylated and bound covalently to the peptidyl carrier protein (PCP). Then, the upstream or downstream condensation domain catalyzes the peptide bond formation. Ending the mechanism, the terminal tioestherase domain catalyzes the peptide release (Mitchell et al. 2012). Normally, this latter step is responsible for the cyclization of mature lipopeptides (Samel. et al. 2006).