METABOLITES OF ERWINIA .10. METABOLISM OF POLYAMINES AND BASIC-AMINO-ACIDS IN ERWINIA-AMYLOVORA - APPLICATION OF LIQUID-CHROMATOGRAPHY ELECTROSPRAY MASS-SPECTROMETRY TO PROFERRIOXAMINE PRECURSOR FEEDING AND INHIBITION STUDIES
Gj. Feistner, METABOLITES OF ERWINIA .10. METABOLISM OF POLYAMINES AND BASIC-AMINO-ACIDS IN ERWINIA-AMYLOVORA - APPLICATION OF LIQUID-CHROMATOGRAPHY ELECTROSPRAY MASS-SPECTROMETRY TO PROFERRIOXAMINE PRECURSOR FEEDING AND INHIBITION STUDIES, Biological mass spectrometry, 23(12), 1994, pp. 793-803
Erwinia amylovora, the etiological agent of fire blight, produces a fa
mily of proferrioxamine siderophores, which may be essential for the p
athogen to establish itself in its hosts, If so, then control of fire
blight may perhaps be possible via interference with proferrioxamine b
iosynthesis. Proof of this hypothesis requires prior knowledge of the
corresponding biosynthetic pathways in E. amylovora, As a first step t
owards understanding proferrioxamine biosynthesis, it was of interest
to investigate the ability of the fire blight bacterium to utilize var
ious potential biosynthetic pathways for diamines, Feeding of lysine,
ornithine and diaminobutyric acid gave rise to highly elevated levels
of cadaverine, putrescine and diaminopropane, respectively, indicating
that the corresponding decarboxylase activities are all present in E.
amylovora, The conclusion for lysine decarboxylase was confirmed with
(N-15(2))lysine, which was converted to (N-15(2))cadaverine. Arginine
did not increase putrescine levels substantially, but (C-13(6))argini
ne nevertheless gave rise to (C-13(4))putrescine while suppressing exc
retion of non-labeled putrescine, A serendipitous result of this study
was the finding that the growth of E, amylovora can be inhibited with
5-hydroxylysine and 1,4-diamino-2-butanone. The mechanism of inhibiti
on appears complex and is not yet understood, For 5-hydroxylysine, pre
liminary investigations point to a competitive inhibition of lysine de
carboxylase, However, the growth inhibition cannot be reversed by prov
iding cadaverine, the decarboxylation product of lysine,