Chymotrypsin modified with polyethylene glycol catalyzes peptide synthesis reaction in benzene.
Chymotrypsin was modified in the zymogen form with 2,4-bis(O-methoxypolyethylene glycol)-6-chloro-s-triazine (activated PEG2), followed by activation with trypsin. The modified enzyme was soluble in benzene and retained its enzymic activity. Acid-amide bond formation by the modified enzyme proceeded efficiently in benzene: N-benzoyltyrosine butylamide was made from N-benzoyl-L-tyrosine ethyl ester and n-butylamine, and benzoyltyrosine(oligo)phenylalanine ethyl esters were formed from N-benzoyl-L-tyrosine ethyl ester and L-phenylalanine ethyl ester.
D000818:Animals; D001554:Benzene; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D002918:Chymotrypsin / Q000378:metabolism*; D004789:Enzyme Activation / Q000187:drug effects; D010452:Peptide Biosynthesis; D010649:Phenylalanine / Q000031:analogs & derivatives / Q000096:biosynthesis; D011092:Polyethylene Glycols / Q000494:pharmacology*; D012995:Solubility; D014357:Trypsin / Q000494:pharmacology; D014443:Tyrosine / Q000031:analogs & derivatives / Q000096:biosynthesis
D011092:Polyethylene Glycols; D014443:Tyrosine; D010649:Phenylalanine; C029761:2,4-bis(O-methoxypolyethylene glycol)-6-chloro-s-triazine; C043298:N-benzoyltyrosine butylamide; D002918:Chymotrypsin; D014357:Trypsin; D001554:Benzene