{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Calderone CT"],"funding":["NIAID NIH HHS","NIGMS NIH HHS"],"pagination":["835-46"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2084360"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["14(7)"],"pubmed_abstract":["Several polyketide secondary metabolites are predicted to undergo isoprenoid-like beta-alkylations during biosynthesis. One such secondary metabolite is myxovirescin A1, produced by Myxococcus xanthus. Myxovirescin is of special interest in that it appears to undergo two distinct beta-alkylations. Additionally, the myxovirescin biosynthetic gene cluster lacks tandem thiolation domains required in the synthesis of other beta-branched secondary metabolites. To probe the origins of the beta-branches in myxovirescin, we heterologously overexpressed the proteins predicted to be responsible for myxovirescin beta-alkylation and reconstituted their activities in vitro on model substrates. Our results confirm that myxovirescin undergoes two isoprenoid-like beta-alkylations during its biosynthesis, "],"journal":["Chemistry & biology"],"pubmed_title":["Incorporation of nonmethyl branches by isoprenoid-like logic: multiple beta-alkylation events in the biosynthesis of myxovirescin A1."],"pmcid":["PMC2084360"],"funding_grant_id":["GM067725","GM073323","AI042738","R01 AI042738","F32 GM020011","F32 GM073323","GM020011","GM081743","R01 GM020011","F32 GM081743","R01 GM067725"],"pubmed_authors":["Iwig DF","Walsh CT","Dorrestein PC","Kelleher NL","Calderone CT"],"additional_accession":[]},"is_claimable":false,"name":"Incorporation of nonmethyl branches by isoprenoid-like logic: multiple beta-alkylation events in the biosynthesis of myxovirescin A1.","description":"Several polyketide secondary metabolites are predicted to undergo isoprenoid-like beta-alkylations during biosynthesis. One such secondary metabolite is myxovirescin A1, produced by Myxococcus xanthus. Myxovirescin is of special interest in that it appears to undergo two distinct beta-alkylations. Additionally, the myxovirescin biosynthetic gene cluster lacks tandem thiolation domains required in the synthesis of other beta-branched secondary metabolites. To probe the origins of the beta-branches in myxovirescin, we heterologously overexpressed the proteins predicted to be responsible for myxovirescin beta-alkylation and reconstituted their activities in vitro on model substrates. Our results confirm that myxovirescin undergoes two isoprenoid-like beta-alkylations during its biosynthesis, ","dates":{"release":"2007-01-01T00:00:00Z","publication":"2007 Jul","modification":"2026-05-02T20:53:36.607Z","creation":"2019-03-27T02:22:00Z"},"accession":"S-EPMC2084360","cross_references":{"pubmed":["17656320"],"doi":["10.1016/j.chembiol.2007.06.008"]}}