Abstract: The present invention provides for a cyclopropane compound having the following chemical formula: wherein ? is —H or —COOR, wherein R is —H or an alkyl group, such as —CH3, —CH2CH3, —(CH2)2—CH3, —(CH2)3—CH3, or —C(CH3)3; ? is each independently wherein at least one ? is and, n is an integer from 3 to 11. A fuel composition comprising the cyclopropane compound thereof and a fuel additive. The present invention also provides for a system or genetically modified host cell capable of producing the cyclopropane compound, and a method for producing the cyclopropane compound.

Abstract: The present invention describes a new peptide aldehyde produced naturally by Streptomyces lividans 66, which we have called livipeptin. Using genome mining of natural products, we predicted that SLI0883-5 genes encode an unprecedented biosynthetic system, unusually small (4.6 Kbp), which produces an acylated peptide aldehyde. Because of the chemical characteristics of the predicted compound, we postulated its anti-proteolytic activity, which we confirmed by identifying and purifying this compound through metabolic profiles of HPLC and MS of the mutated strain lacking these three genes and the wild strain. To this objective, we identified the conditions wherein these genes are strongly expressed. The livipeptin was purified and its inhibitory activity on the proteolytic activity of selected proteases was demonstrated in vitro. The design of an expression cassette for its heterologous expression is also described plus its use for heterologous protein production.

Abstract: The present invention describes a new peptide aldehyde produced naturally by Streptomyces lividans 66, which we have called livipeptin. Using genome mining of natural products, we predicted that SLl0883-5 genes encode an unprecedented biosynthetic system, unusually small (4.6 Kbp), which produces an acylated peptide aldehyde. Because of the chemical characteristics of the predicted compound, we postulated its anti-proteolytic activity, which we confirmed by identifying and purifying this compound through metabolic profiles of HPLC and MS of the mutated strain lacking these three genes and the wild strain. To this objective, we identified the conditions wherein these genes are strongly expressed. The livipeptin was purified and its inhibitory activity on the proteolytic activity of selected proteases was demonstrated in vitro. The design of an expression cassette for its heterologous expression is also described plus its use for heterologous protein production.