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Article

Functional characterization of an aminotransferase required for pyoverdine siderophore biosynthesis in Pseudomonas aeruginosa PAO1.

Journal of bacteriology - 1 Sept 2004

Vandenende Chris S, Vlasschaert Matthew, Seah Stephen Y K

Abstract excerpt

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 beta-semialdehyde dehydrogenase) knockout mutants of Pseudomonas aeruginosa PAO1 were unable to synthesize pyoverdine under iron-limiting conditions in the absence of l-2,4-diaminobutyrate in the culture media. The pvdH...

Topics

Aminobutyrates
Aspartate-Semialdehyde Dehydrogenase
Aspartic Acid
Bacterial Proteins
Cloning, Molecular
Gene Deletion
Genes, Bacterial
Ketoglutaric Acids
Mutagenesis, Insertional
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Oligopeptides

Pigments, Biological

Pseudomonas

Pseudomonas aeruginosa

Sequence Homology

Substrate Specificity

Synteny

Transaminases

Source

Open in PubMed Open full text

Identifiers

PMID: 15317763
DOI: 10.1128/JB.186.17.5596-5602.2004
PMCID: PMC516838

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