Open AccessBiosynthesis of desferrioxamine B in Streptomyces pilosus : Evidence for the involvement of lysine decarboxylase
Author(s) -
Schupp T.,
Waldmeier U.,
Divers M.
Publication year - 1987
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1987.tb02060.x
Subject(s) - biosynthesis , biochemistry , lysine decarboxylase , lysine , enzyme , carboxy lyases , uroporphyrinogen iii decarboxylase , biology , siderophore , mutant , chemistry , amino acid , gene , spermine , heme , cadaverine
Lysine decarboxylase activity (E.C. 4.1.1.18) was demonstrated in crude extracts of Streptomyces pilosus and evidence obtained for its involvement in biosynthesis of the siderophore desferrioxamine B. Appearance of enzyme activity in growing cultures correlated well with productivity of desferrioxamine B. One class of mutants blocked in biosynthesis showed no lysine decarboxylase activity, and feeding of the enzyme product restored biosynthesis. Mutants with increased desferrioxamine B production showed increased enzyme activity. Both desferrioxamine B biosynthesis and lysine decarboxylase activity were regulated by iron, and for the latter this was found to occur by repression of enzyme synthesis.