Abstract | BACKGROUND: RESULTS: CONCLUSIONS: The HMWP1 and HMWP2 domain organization suggests that the yersiniabactin siderophore is assembled in a modular fashion, in which a series of covalent intermediates are passed from the amino terminus of HMWP2 to the carboxyl terminus of HMWP1. Biosynthetic labeling studies indicate that the three yersiniabactin methyl moieties are donated by S-adenosylmethionine and that the linker between the thiazoline and thiazolidine rings is derived from malonyl-CoA. The salicylate moiety is probably synthesized using the aromatic amino-acid biosynthetic pathway, the final step of which converts chorismate to salicylate. YbtS might be necessary for converting chorismate to salicylate.
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Authors | A M Gehring, E DeMoll, J D Fetherston, I Mori, G F Mayhew, F R Blattner, C T Walsh, R D Perry |
Journal | Chemistry & biology
(Chem Biol)
Vol. 5
Issue 10
Pg. 573-86
(Oct 1998)
ISSN: 1074-5521 [Print] United States |
PMID | 9818149
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)
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Chemical References |
- Bacterial Outer Membrane Proteins
- Bacterial Proteins
- DNA Primers
- Iron-Binding Proteins
- Multienzyme Complexes
- Periplasmic Binding Proteins
- Phenols
- Siderophores
- Thiazoles
- yersiniabactin
- Iron
- Salicylic Acid
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Topics |
- Amino Acid Sequence
- Bacterial Outer Membrane Proteins
- Bacterial Proteins
(chemistry, metabolism)
- Base Sequence
- DNA Primers
- Iron
(metabolism)
- Iron-Binding Proteins
- Molecular Sequence Data
- Multienzyme Complexes
(metabolism)
- Periplasmic Binding Proteins
- Phenols
- Plague
(metabolism)
- Salicylic Acid
(metabolism)
- Sequence Homology, Amino Acid
- Siderophores
(biosynthesis)
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
- Thiazoles
- Virulence
- Yersinia pestis
(metabolism, pathogenicity)
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