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10.1074/jbc.M116.722108 http://scihub22266oqcxt.onion/10.1074/jbc.M116.722108 C4919450!4919450!27151214     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Biol+Chem 2016 ; 291 (26): 13662-78 Nephropedia Template TP {{tp|p=27151214|t=2016. Insights into the Unique Phosphorylation of the Lasso Peptide Paeninodin* |pdf=|usr=}}{{27151214}} gab.com Text Insights into the Unique Phosphorylation of the Lasso Peptide Paeninodin* JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=27151214 #FOAvip Lasso peptides are a new class of ribosomally synthesized and post-translationally modified peptides and thus far are only isolated from proteo- and actinobacterial sources. Typically, lasso peptide biosynthetic gene clusters encode enzymes for biosynthesis and export but not for tailoring. Here, we describe the isolation of the novel lasso peptide paeninodin from the firmicute Paenibacillus dendritiformis C454 and reveal within its biosynthetic cluster a gene encoding a kinase, which we have characterized as a member of a new class of lasso peptide-tailoring kinases. By employing a wide variety of peptide substrates, it was shown that this novel type of kinase specifically phosphorylates the C-terminal serine residue while ignoring those located elsewhere. These experiments also reveal that no other recognition motif is needed for efficient enzymatic phosphorylation of the C-terminal serine. Furthermore, through comparison with homologous HPr kinases and subsequent mutational analysis, we confirmed the essential catalytic residues. Our study reveals how lasso peptides are chemically diversified and sets the foundation for rational engineering of these intriguing natural products. Twit Text FOAVip Insights into the Unique Phosphorylation of the Lasso Peptide Paeninodin* ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=27151214 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27151214 #FOAvip English Wikipedia <ref>{{Cite pmid|27151214}}</ref> Insights into the Unique Phosphorylation of the Lasso Peptide Paeninodin* #MMPMID27151214 Zhu S; Hegemann JD; Fage CD; Zimmermann M; Xie X; Linne U; Marahiel MA J Biol Chem 2016[Jun]; 291 (26): 13662-78 PMID27151214show ga Lasso peptides are a new class of ribosomally synthesized and post-translationally modified peptides and thus far are only isolated from proteo- and actinobacterial sources. Typically, lasso peptide biosynthetic gene clusters encode enzymes for biosynthesis and export but not for tailoring. Here, we describe the isolation of the novel lasso peptide paeninodin from the firmicute Paenibacillus dendritiformis C454 and reveal within its biosynthetic cluster a gene encoding a kinase, which we have characterized as a member of a new class of lasso peptide-tailoring kinases. By employing a wide variety of peptide substrates, it was shown that this novel type of kinase specifically phosphorylates the C-terminal serine residue while ignoring those located elsewhere. These experiments also reveal that no other recognition motif is needed for efficient enzymatic phosphorylation of the C-terminal serine. Furthermore, through comparison with homologous HPr kinases and subsequent mutational analysis, we confirmed the essential catalytic residues. Our study reveals how lasso peptides are chemically diversified and sets the foundation for rational engineering of these intriguing natural products. äInsights into the Unique Phosphorylation of the Lasso Peptide Paeninod(epmc).pdf DeepDyve Pubget Overpricing