Formation of D-Phe-Pro-Val-cyclo-Orn by gramicidin S synthetase in the absence of L-leucine.
The preparation of both enzymes of gramicidin S synthetase was efficiently improved by introduction of the fast protein liquid chromatography technique. High-resolution anion-exchange chromatography on Pharmacia Mono Q HR 5/5 was used as the final purification step. D-Phe-Pro-Val-cyclo-Orn was obtained as a product of the multienzyme by omission of L-leucine from the complete bioassay mixture. This tetrapeptide was formed by cyclization of the C-terminal ornithine to 3-amino-2-piperidone. It was identified and characterized by chromatographic and spectroscopic procedures using chemically synthesized reference compounds.
D000591:Amino Acid Isomerases / Q000302:isolation & purification / Q000378:metabolism*; D002852:Chromatography, Ion Exchange; D002853:Chromatography, Liquid / Q000379:methods; D002855:Chromatography, Thin Layer; D003500:Cyclization; D007700:Kinetics; D009097:Multienzyme Complexes / Q000302:isolation & purification / Q000378:metabolism*; D010453:Peptide Synthases / Q000302:isolation & purification / Q000378:metabolism*; D010456:Peptides, Cyclic / Q000096:biosynthesis*
D009097:Multienzyme Complexes; D010456:Peptides, Cyclic; C051645:cyclo(ornithyl)phenylalanyl-prolyl-valine; D000591:Amino Acid Isomerases; D010453:Peptide Synthases; C020831:gramicidin-S-synthetase 2