Precursor activation in a pyoverdine biosynthesis
The siderophore produced by Azotobacter vinelandii strain UW belongs to a large family of peptidic siderophores collectively called pyoverdines. The biosynthesis of the peptidyl moiety of this siderophore was shown to involve activation of the constituent amino acids as their adenylates, as demonstr...
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Published in | Biochimica et biophysica acta Vol. 1038; no. 1; pp. 47 - 51 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Amsterdam
Elsevier B.V
29.03.1990
Elsevier North-Holland |
Subjects | |
Online Access | Get full text |
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Summary: | The siderophore produced by
Azotobacter vinelandii strain UW belongs to a large family of peptidic siderophores collectively called pyoverdines. The biosynthesis of the peptidyl moiety of this siderophore was shown to involve activation of the constituent amino acids as their adenylates, as demonstrated by amino acid-dependent ATP-[
32P]pyrophosphate exchange. The enzyme system responsible for this activation was partially purified by chromatographic techniques. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0167-4838 0006-3002 1879-2588 1878-2434 |
DOI: | 10.1016/0167-4838(90)90008-4 |