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10.1021/cb5009876 http://scihub22266oqcxt.onion/10.1021/cb5009876 C4414810!4414810!25619528     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       ACS+Chem+Biol 2015 ; 10 (4): 970-7 Nephropedia Template TP {{tp|p=25619528|t=2015. Synergistic binding of the leader and core peptides by the lantibiotic synthetase HalM2 |pdf=|usr=}}{{25619528}} gab.com Text Synergistic binding of the leader and core peptides by the lantibiotic synthetase HalM2 JO: ACS Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=25619528 #FOAvip Lanthipeptides are a class of ribosomally-produced and post-translationally modified peptides (RiPPs) that possess a variety of biological activities, but typically act as antimicrobial agents (lantibiotics). Haloduracin is a lantibiotic that is composed of two post-translationally modified peptides, Hal? and Hal?, which are biosynthesized from the precursor peptides HalA1 and HalA2 by their cognate lanthipeptide synthetases, HalM1 and HalM2, respectively. Co-expression studies of HalM1 and HalM2 with chimeric peptides consisting of the leader peptide of HalA1 and the core peptide of HalA2 (or vice versa) showed that the synthetases require both the cognate leader and core peptides for efficient processing. Investigation of the affinity in vitro showed that binding of the N-terminal leader peptide by HalM2 increases its affinity for the C-terminal core peptide. Thus, the two segments of the precursor peptide HalA2 synergistically bind to HalM2. Twit Text FOAVip Synergistic binding of the leader and core peptides by the lantibiotic synthetase HalM2 ????ACS Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=25619528 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25619528 #FOAvip English Wikipedia <ref>{{Cite pmid|25619528}}</ref> Synergistic binding of the leader and core peptides by the lantibiotic synthetase HalM2 #MMPMID25619528 Thibodeaux GN; McClerren AL; Ma Y; Gancayco MR; van der Donk WA ACS Chem Biol 2015[Apr]; 10 (4): 970-7 PMID25619528show ga Lanthipeptides are a class of ribosomally-produced and post-translationally modified peptides (RiPPs) that possess a variety of biological activities, but typically act as antimicrobial agents (lantibiotics). Haloduracin is a lantibiotic that is composed of two post-translationally modified peptides, Hal? and Hal?, which are biosynthesized from the precursor peptides HalA1 and HalA2 by their cognate lanthipeptide synthetases, HalM1 and HalM2, respectively. Co-expression studies of HalM1 and HalM2 with chimeric peptides consisting of the leader peptide of HalA1 and the core peptide of HalA2 (or vice versa) showed that the synthetases require both the cognate leader and core peptides for efficient processing. Investigation of the affinity in vitro showed that binding of the N-terminal leader peptide by HalM2 increases its affinity for the C-terminal core peptide. Thus, the two segments of the precursor peptide HalA2 synergistically bind to HalM2. äSynergistic binding of the leader and core peptides by the lantibiotic(epmc).pdf DeepDyve Pubget Overpricing