Abstract
The important biological macromolecules, such as lipopeptide and glycolipid biosurfactant producing marine actinobacteria were analyzed and their potential linkage between type II polyketide synthase (PKS) genes was explored. A unique feature of type II PKS genes is their high amino acid (AA) sequence homology and conserved gene organization. These enzymes mediate the biosynthesis of polyketide natural products with enormous structural complexity and chemical nature by combinatorial use of various domains. Therefore, deciphering the order of AA sequence encoded by PKS domains tailored the chemical structure of polyketide analogs still remains a great challenge. The present work deals with an in vitro and in silico analysis of PKS type II genes from five actinobacterial species to correlate KS domain architecture and structural features. Our present analysis reveals the unique protein domain organization of iterative type II PKS and KS domain of marine actinobacteria. The findings of this study would have implications in metabolic pathway reconstruction and design of semi-synthetic genomes to achieve rational design of novel natural products.
Highlights
Natural products of microorganisms are potential source of bioactives that have been extensively exploited to develop generation anti-infective drugs proposed by pharmaceutical companies (De Carvalho and Fernandes, 2010)
The actinobacterial isolates from marine sponges were screened for biosurfactant activity using emulsification index (E24) as per Kiran et al (2010)
MSA21 were evidenced as biosurfactant molecules, but the moieties of MAD01 and MSI051 were not related with biosurfactants (Table 2)
Summary
Natural products of microorganisms are potential source of bioactives that have been extensively exploited to develop generation anti-infective drugs proposed by pharmaceutical companies (De Carvalho and Fernandes, 2010). Analysis of Polyketide Synthase Genes and microbial isolates were tremendously increased, the leads transformed to drugs are very few (Watve et al, 2001). Perhaps this trend might have led to the exploration of pristine and unexplored bioresources including hydrothermal vents and extreme niches. Exploration of sponge associated microbial diversity and symbiont-assisted complex biosynthetic pathway of bioactive leads have increased the scope of natural product discovery from marine sponges (Faulkner and Ghiselin, 1983, 1994; Hentschel et al, 2002). The sponge-derived bioactive peptides are nonribosomal origin and are modified with unusual amino acids (AAs; Matsunaga et al, 1985)
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