{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Christiansen G"],"funding":["Austrian Science Fund FWF","NIEHS NIH HHS"],"pagination":["3822-31"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3147517"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["193(15)"],"pubmed_abstract":["Anabaenopeptins (AP) are bioactive cyclic hexapeptides synthesized nonribosomally in cyanobacteria. APs are characterized by several conserved motifs, including the ureido bond, N-methylation in position 5, and d-Lys in position 2. All other positions of the AP molecule are variable, resulting in numerous structural variants. We have identified a nonribosomal peptide synthetase (NRPS) operon from Planktothrix agardhii strain CYA126/8 consisting of five genes (apnA to apnE) encoding six NRPS modules and have confirmed its role in AP synthesis by the generation of a mutant via insertional inactivation of apnC. In order to correlate the genetic diversity among adenylation domains (A domains) with AP structure variation, we sequenced the A domains of all six NRPS modules from seven Planktothri"],"journal":["Journal of bacteriology"],"pubmed_title":["Genetic variation of adenylation domains of the anabaenopeptin synthesis operon and evolution of substrate promiscuity."],"pmcid":["PMC3147517"],"funding_grant_id":["P50ES012740","P 20231","P50 ES012740"],"pubmed_authors":["Hemscheidt T","Christiansen G","Kurmayer R","Philmus B"],"additional_accession":[]},"is_claimable":false,"name":"Genetic variation of adenylation domains of the anabaenopeptin synthesis operon and evolution of substrate promiscuity.","description":"Anabaenopeptins (AP) are bioactive cyclic hexapeptides synthesized nonribosomally in cyanobacteria. APs are characterized by several conserved motifs, including the ureido bond, N-methylation in position 5, and d-Lys in position 2. All other positions of the AP molecule are variable, resulting in numerous structural variants. We have identified a nonribosomal peptide synthetase (NRPS) operon from Planktothrix agardhii strain CYA126/8 consisting of five genes (apnA to apnE) encoding six NRPS modules and have confirmed its role in AP synthesis by the generation of a mutant via insertional inactivation of apnC. In order to correlate the genetic diversity among adenylation domains (A domains) with AP structure variation, we sequenced the A domains of all six NRPS modules from seven Planktothri","dates":{"release":"2011-01-01T00:00:00Z","publication":"2011 Aug","modification":"2026-04-30T20:03:33.495Z","creation":"2019-03-27T03:07:35Z"},"accession":"S-EPMC3147517","cross_references":{"pubmed":["21622740"],"doi":["10.1128/jb.00360-11","10.1128/JB.00360-11"]}}