id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-013952-zp4q3ztr	Moll, Gert N.	Biosynthesis of lanthionine-constrained agonists of G protein-coupled receptors	2020-10-30		.txt	text/plain	3937	209	40	Biosynthesis of lanthionine-constrained peptides exploiting engineered Gram-positive or Gram-negative bacteria that contain lanthionine-introducing enzymes constitutes a convenient method for discovery of lanthionine-stabilized GPCR agonists. The nisin precursor peptide is dehydrated by the dehydratase NisB [26, 27] , after which a cyclase NisC [28] couples dehydroamino acids to cysteines followed by export by the transporter NisT and removal of the leader peptide by the extracellular leader peptidase NisP [29] . While the attainment of strict rules with respect to the substrate specificities of lanthionine-introducing enzymes has been challenging, some practical guidelines for the design of modifiable peptides have been reached for some lanthipeptide biosynthesis systems [32] . The stereospecificity of NisC-cyclized GPCR agonist, 4,7 lanthionine-angiotensin-(1-7) was investigated using the Ni 2 B method, which opens the ring structure while retaining the D or L conformation [43] . In addition, the feasibility of highthroughput screening for tailor-made lanthionine-introducing enzymes with adapted substrate specificity for rational design and biosynthesis of lanthipeptide GPCR agonists has recently been demonstrated.	./cache/cord-013952-zp4q3ztr.txt	./txt/cord-013952-zp4q3ztr.txt