title: Enzyme-bound formylvaline and formylvalylglycine; an initiation complex for gramicidin A biosynthesis.
abstract: Gramicidin A is an antibiotic peptide produced by Bacillus brevis ATCC 8185, which also produces tyrocidines. An attempt was made to establish a cell-free enzyme system for gramicidin A synthesis. An enzyme fraction, Component I, was partially purified from crude extracts of the organism and proven to be involved in the synthesis of the formyl-Val-Gly- region of gramicidin A. The initiation of gramicidin A biosynthesis is a function of Component I, which activates valine and binds it as a thioester, and further formylates it in the presence of formyltetrahydrofolic acid. The formylvaline thus synthesized is transferred to the glycine moiety, which is also thioesterified to Component I. Elongation of the peptide chain takes place by a mechanism similar to those found for tyrocidines, gramicidin S, and bacitracin.
mesh_terms: D049148:Aminoacylation; D001407:Bacillus / Q000201:enzymology / Q000378:metabolism*; D002474:Cell-Free System; D004151:Dipeptides / Q000096:biosynthesis; D005561:Formates / Q000378:metabolism*; D005998:Glycine / Q000031:analogs & derivatives; D006096:Gramicidin / Q000096:biosynthesis*; D010441:Peptide Chain Elongation, Translational; D014633:Valine / Q000031:analogs & derivatives* / Q000378:metabolism
chemical_list: D004151:Dipeptides; D005561:Formates; D006096:Gramicidin; C014563:formylvaline; D014633:Valine; D005998:Glycine