Commercialization as a Tool for the Conservation of Environmental Resources

The primary objective of the paper is to report the survey of environmental resources conducted in Ode-Irele forest using two staged technique. This study was framed within the model that sustainable management of environmental resources is a consequence of heavy reliance on subsistence extraction of resources. Data were analysed using descriptive statistics of frequency counts and percentages. The result reveals that 65% of the respondents hunted wild animals for food, 62% also traded in wild animals and their products, 69% traded in natural honey, and 86% also traded in medicinal plants. 92% of respondents were involved in collecting wood for use and sale, while 92% were also involved in trade in wild fruits. Most of the respondents, who hunted animals for food, traded in wild animals and their products, natural honey, medicinal plants, wild fruits and those who also collected firewood for use and sale also conserved trees on their farms for the continued availability of the resources. Sustainable use of environmental resources by local residents in natural forested areas could only be achieved if they realize that continued availability of the resources is dependent upon the wise use and most importantly the conservation of the resources

Identification of polyketide inhibitors targeting 3-dehydroquinate dehydratase in the shikimate pathway of Enterococcus faecalis.

Due to the emergence of resistance toward current antibiotics, there is a pressing need to develop the next generation of antibiotics as therapeutics against infectious and opportunistic diseases of microbial origins. The shikimate pathway is exclusive to microbes, plants and fungi, and hence is an attractive and logical target for development of antimicrobial therapeutics. The Gram-positive commensal microbe, Enterococcus faecalis, is a major human pathogen associated with nosocomial infections and resistance to vancomycin, the "drug of last resort". Here, we report the identification of several polyketide-based inhibitors against the E. faecalis shikimate pathway enzyme, 3-dehydroquinate dehydratase (DHQase). In particular, marein, a flavonoid polyketide, both inhibited DHQase and retarded the growth of Enterococcus faecalis. The purification, crystallization and structural resolution of recombinant DHQase from E. faecalis (at 2.2 Å resolution) are also reported. This study provides a route in the development of polyketide-based antimicrobial inhibitors targeting the shikimate pathway of the human pathogen E. faecalis

Double-reciprocal plots for three of the identified inhibitors targeting efDHQase.

<p>Plot for aesculine (A) and marein (B) showing two possible scenarios for mixed inhibition where the lines intersect either below the x-axis or just after y-axis respectively. Plot for rutin (C) showing uncompetitive inhibition where the lines run parallel to one another.</p

efDHQase inhibition constants (<i>K</i>_I).

<p>efDHQase inhibition constants (<i>K</i>_I).</p

Backbone structure of flavones.

<p>Two benzene rings (A and B) linked through a heterocyclic pyrane ring (C).</p

List of flavonoids inhibiting <i>Enterococcus faecalis</i>.

<p>List of flavonoids inhibiting <i>Enterococcus faecalis</i>.</p

Data Collection, Refinement and Structure Validation Statistics.

<p>Data Collection, Refinement and Structure Validation Statistics.</p

Crystal structure of efDHQase.

<p>The biological assembly of efDHQase is a homodimer. Alpha-helices, β-strands, and loops are shown as cartoon representations and colored light blue, golden, and pink, respectively, to visualize the (β/α)₈-barrel scaffold on each monomer. Residues at the dimer interface are highlighted purple on the surface (grey) of one monomer. Residues involved in ligand binding are shown as sticks and colored cyan. Comparison of efDHQase's active center with homologous 3-dehydroquinate dehydratases from <i>Salmonella enterica</i> (seDHQase) and <i>Clostridium difficile</i> (cdDHQase) is shown in the magnified view on the right. The structures were superimposed onto each other using the Cα atoms of the ligand-binding residues, with the residues from seDHQase and cdDHQase colored dark green and yellow, respectively. The pre-dehydration intermediate covalently-attached to seDHQase is drawn as green sticks. Part of the β8-α8 loop from seDHQase is shown as light green cartoon representations.</p

Kinetic parameters of various DHQases.

<p>Kinetic parameters of various DHQases.</p

efSHD-diaphorase coupled-enzyme assay.

<p>efSHD-diaphorase coupled-enzyme assay.</p