The invention relates to a polypeptide for the enzymatic detoxification of zearalenone, said polypeptide being a monooxygenase which converts the keto group in position 7 of zearalenone into an ester group, the monooxygenase in particular being an amino acid sequence selected from the group comprising sequence ID No. 1, 2 and 3 or a functional variant thereof. The functional variant and at least one of the amino acid sequences has a sequence identity of at least 60%, preferably at least 70%, more preferably at least 80% and most preferably 90%,

Provided herein are methods, compositions, and non-naturally occurring microbial organism for preparing compounds such as1-butanol, butyric acid, succinic acid, 1,4-butanediol, 1-pentanol, pentanoic acid, glutaric acid, 1,5-pentanediol, 1-hexanol, hexanoic acid, adipic acid, 1,6-hexanediol, 6-hydroxy hexanoic acid, ?-Caprolactone, 6-amino-hexanoic acid, ?-Caprolactam, hexamethylenediamine, linear fatty acids and linear fatty alcohols that are between 7-25 carbons long, linear alkanes and linear ?-alkenes that are between 6-24 carbons long, sebacic acid and dodecanedioic acid comprising: a) converting a C.sub.N aldehyde and pyruvate to a C.sub.N+3 ?-hydroxyketone intermediate through an aldol addition; and b) converting the C.sub.N+3 ?-hydroxyketone intermediate to the compounds through enzymatic steps, or a combination of enzymatic and chemical steps.

Provided herein are methods, compositions, and non-naturally occurring microbial organism for preparing compounds such as1-butanol, butyric acid, succinic acid, 1,4-butanediol, 1-pentanol, pentanoic acid, glutaric acid, 1,5-pentanediol, 1-hexanol, hexanoic acid, adipic acid, 1,6-hexanediol, 6-hydroxy hexanoic acid, ?-Caprolactone, 6-amino-hexanoic acid, ?-Caprolactam, hexamethylenediamine, linear fatty acids and linear fatty alcohols that are between 7-25 carbons long, linear alkanes and linear ?-alkenes that are between 6-24 carbons long, sebacic acid and dodecanedioic acid comprising: a) converting a C.sub.N aldehyde and pyruvate to a C.sub.N+3 ?-hydroxyketone intermediate through an aldol addition; and b) converting the C.sub.N+3 ?-hydroxyketone intermediate to the compounds through enzymatic steps, or a combination of enzymatic and chemical steps.

An enzyme with an acyl transfer function has an amino acid sequence identical to a SEQ ID NO:1, which is capable of acylation modification for macrolactins, filipins macrolides, chloramphenicol, and glycosylated piericidin A. An application of an acyltransferase of the present invention is to bind an acyl group of an acyl donor to macrolide compounds, chloramphenicol and glycosylated piericidins. The enzyme with the acyl transfer function can improve pharmacological activity of the macrolide compounds through acylation reaction of macrolactins, thereby improving bioavailability, enhancing efficacy, and reducing toxic as well as side effects, which provides a new strategy for the drug development of macrolide compounds.

An enzyme with an acyl transfer function has an amino acid sequence identical to a SEQ ID NO:1, which is capable of acylation modification for macrolactins, filipins macrolides, chloramphenicol, and glycosylated piericidin A. An application of an acyltransferase of the present invention is to bind an acyl group of an acyl donor to macrolide compounds, chloramphenicol and glycosylated piericidins. The enzyme with the acyl transfer function can improve pharmacological activity of the macrolide compounds through acylation reaction of macrolactins, thereby improving bioavailability, enhancing efficacy, and reducing toxic as well as side effects, which provides a new strategy for the drug development of macrolide compounds.

In this invention, cell lines are created for enzyme inhibitory testing of inhibitors against Plasmodium falciparum DHFR-TS and HPPK-DHPS. Provided the complementing DHFR-TS and HPPK-DHPS have sufficient activities to support growth of the surrogates in un-supplemented medium, the same surrogates could be used for screening inhibitors of targets against other parasite and pathogen species e.g. Plasmodium vivax, Trypanosoma brucei, Trypanosoma cruzi, Toxoplasma gondii or Mycobacterium tuberculosis. The cell lines in this invention are Escherichia coli strain whose thyA, folA, folK, and folP genes were disrupted using genetic knockout coupled with elimination of antibiotic resistance markers. The thyA KO, folP KO, folK KO, thyAfolA KO, folKfolP KO, thyAfolAfolP KO, thyAfolAfolK KO and thyAfolAfolKfolP KO E. coli cell lines are easy and convenient for testing single and combination drugs as plasmids bearing complementing parasite genes can be introduced simply by transformation using standard antibiotic selection.

A method for increasing the molecular diversity of polyketides and non-ribosomal peptides by using recombination to efficiently increase or decrease the number of modules in the polyketide synthase or non-ribosomal peptide synthetase encoding the polyketide or peptide.

A method for increasing the molecular diversity of polyketides and non-ribosomal peptides by using recombination to efficiently increase or decrease the number of modules in the polyketide synthase or non-ribosomal peptide synthetase encoding the polyketide or peptide.

The invention provides non-naturally occurring microbial organisms containing caprolactone pathways having at least one exogenous nucleic acid encoding a butadiene pathway enzyme expressed in a sufficient amount to produce caprolactone. The invention additionally provides methods of using such microbial organisms to produce caprolactone by culturing a non-naturally occurring microbial organism containing caprolactone pathways as described herein under conditions and for a sufficient period of time to produce caprolactone.

The invention provides non-naturally occurring microbial organisms containing caprolactone pathways having at least one exogenous nucleic acid encoding a butadiene pathway enzyme expressed in a sufficient amount to produce caprolactone. The invention additionally provides methods of using such microbial organisms to produce caprolactone by culturing a non-naturally occurring microbial organism containing caprolactone pathways as described herein under conditions and for a sufficient period of time to produce caprolactone.