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Functional Characterization of an Aminotransferase Required for Pyoverdine Siderophore Biosynthesis in Pseudomonas aeruginosa PAO1
The fluorescent dihydroxyquinoline chromophore of the pyoverdine siderophore in Pseudomonas is a condensation product of d-tyrosine and l-2,4-diaminobutyrate. Both pvdH and asd (encoding aspartate β-semialdehyde dehydrogenase) knockout mutants of Pseudomonas aeruginosa PAO1 were unable to synthesize...
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| Hoofdauteurs: | , , |
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| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
American Society for Microbiology
2004
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC516838/ https://ncbi.nlm.nih.gov/pubmed/15317763 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/JB.186.17.5596-5602.2004 |
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