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Inhibition of gramicidin S synthetase 2 by L‐phenylalanine chloromethyl ketone
Author(s) -
Kittelberger Reinhold,
Palacz Zbigniew,
Döhren Hans von,
Salnikow Johann,
Kleinkauf Horst
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80079-9
Subject(s) - gramicidin s , phenylalanine , thioester , stereochemistry , biosynthesis , chemistry , valine , gramicidin , enzyme , biochemistry , leucine , ornithine , amino acid , substrate (aquarium) , biology , arginine , ecology , membrane
The inhibition of the gramicidin S‐biosynthesis and the thioester formation activities of the multienzyme GS 2 by L‐Phe‐CMK, a substrate analogue of L‐phenylalanine, were investigated. L‐Phe‐CMK inhibits irreversibly the activation of proline, valine, ornithine and leucine with about the same velocity and shows no specificity for hydrophobic amino acid binding sites, as could be expected. The gramicidin S‐biosynthesis is inhibited about four times more rapidly than the thioester formation. Prevention of inhibition by the substrates opens the possibility of specific blocking of one or more active sites of the enzyme.