<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Christiansen G</submitter><funding>Austrian Science Fund FWF</funding><funding>NIEHS NIH HHS</funding><pagination>3822-31</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3147517</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>193(15)</volume><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</pubmed_abstract><journal>Journal of bacteriology</journal><pubmed_title>Genetic variation of adenylation domains of the anabaenopeptin synthesis operon and evolution of substrate promiscuity.</pubmed_title><pmcid>PMC3147517</pmcid><funding_grant_id>P50ES012740</funding_grant_id><funding_grant_id>P 20231</funding_grant_id><funding_grant_id>P50 ES012740</funding_grant_id><pubmed_authors>Hemscheidt T</pubmed_authors><pubmed_authors>Christiansen G</pubmed_authors><pubmed_authors>Kurmayer R</pubmed_authors><pubmed_authors>Philmus B</pubmed_authors></additional><is_claimable>false</is_claimable><name>Genetic variation of adenylation domains of the anabaenopeptin synthesis operon and evolution of substrate promiscuity.</name><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</description><dates><release>2011-01-01T00:00:00Z</release><publication>2011 Aug</publication><modification>2026-04-30T20:03:33.495Z</modification><creation>2019-03-27T03:07:35Z</creation></dates><accession>S-EPMC3147517</accession><cross_references><pubmed>21622740</pubmed><doi>10.1128/jb.00360-11</doi><doi>10.1128/JB.00360-11</doi></cross_references></HashMap>