Precursor activation in a pyoverdine biosynthesis

• Published in: Biochimica et biophysica acta Vol. 1038; no. 1; pp. 47 - 51
• Main Authors: Menhart, N., Viswanatha, T.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 29.03.1990; Elsevier; North-Holland
• Subjects: Adenosine Triphosphate - metabolism; Amino Acids - metabolism; Aminoacyl adenylate; Aminoacylation; Azotobacter; Azotobacter - metabolism; Bacteriology; Biological and medical sciences; Diphosphates - metabolism; Fundamental and applied biological sciences. Psychology; Iron Chelating Agents; Microbiology; Miscellaneous; Oligopeptides; Pigments, Biological - biosynthesis; pyoverdin; Pyoverdine; Siderophore; Siderophores; FPLC; AA-tRNA synthetase; Siderophore; Azotobacter; Pyoverdine; PMSF; DTT; Hepes; EDTA; PP i; Aminoacyl adenylate; Purification; Peptides; Enzyme; Activation; Biosynthesis; Azotobacteraceae; Aminoacid; Bacteria; FPLC chromatography; Biosynthesis precursor; Azotobacter vinelandii; Mechanism of action
• ISSN: 0167-4838; 0006-3002; 1879-2588; 1878-2434
• DOI: 10.1016/0167-4838(90)90008-4

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.