dc.identifier.uri |
http://dx.doi.org/10.15488/16333 |
|
dc.identifier.uri |
https://www.repo.uni-hannover.de/handle/123456789/16460 |
|
dc.contributor.author |
Ringel, Michael T.
|
|
dc.contributor.author |
Dräger, Gerald
|
|
dc.contributor.author |
Brüser, Thomas
|
|
dc.date.accessioned |
2024-02-19T08:44:49Z |
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dc.date.available |
2024-02-19T08:44:49Z |
|
dc.date.issued |
2020 |
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dc.identifier.citation |
Ringel, M.T.; Dräger, G.; Brüser, T.: The periplasmic transaminase PtaA of Pseudomonas fluorescens converts the glutamic acid residue at the pyoverdine fluorophore to -ketoglutaric acid. In: Journal of Biological Chemistry, The (JBC) 292 (2020), Nr. 45, S. 18660-18671. DOI: https://doi.org/10.1074/jbc.m117.812545 |
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dc.description.abstract |
The periplasmic conversion of ferribactin to pyoverdine is essential for siderophore biogenesis in fluorescent pseudomonads, such as pathogenic Pseudomonas aeruginosa or plant growth-promoting Pseudomonas fluorescens. The non-ribo-somal peptide ferribactin undergoes cyclizations and oxidations that result in the fluorophore, and a strictly conserved fluorophore-bound glutamic acid residue is converted to a range of variants, including succinamide, succinic acid, and -ketoglu-taric acid residues. We recently discovered that the pyridoxal phosphate-containing enzyme PvdN is responsible for the generation of the succinamide, which can be hydrolyzed to succinic acid. Based on this, a distinct unknown enzyme was postulated to be responsible for the conversion of the glutamic acid to -ke-toglutaric acid. Here we report the identification and characterization of this enzyme in P. fluorescens strain A506. In silico analyses indicated a periplasmic transaminase in fluorescent pseudomonads and other proteobacteria that we termed PtaA for “periplasmic transaminase A.” An in-frame-deleted ptaA mutant selectively lacked the -ketoglutaric acid form of pyoverdine, and recombinant PtaA complemented this phenotype. The ptaA/pvdN double mutant produced exclusively the glutamic acid form of pyoverdine. PtaA is homodimeric and contains a pyridoxal phosphate cofactor. Mutation of the active-site lysine abolished PtaA activity and affected folding as well as Tat-dependent transport of the enzyme. In pseudomonads, the occurrence of ptaA correlates with the occurrence of -ke-toglutaric acid forms of pyoverdines. As this enzyme is not restricted to pyoverdine-producing bacteria, its catalysis of periplasmic transaminations is most likely a general tool for specific biosynthetic pathways. |
eng |
dc.language.iso |
eng |
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dc.publisher |
Bethesda, Md. : ASBMB Publications |
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dc.relation.ispartofseries |
Journal of Biological Chemistry, The (JBC) 292 (2020), Nr. 45 |
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dc.rights |
CC BY 4.0 Unported |
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dc.rights.uri |
https://creativecommons.org/licenses/by/4.0 |
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dc.subject |
Amino Acid Sequence |
eng |
dc.subject |
Amino Acid Substitution |
eng |
dc.subject |
Bacterial Proteins |
eng |
dc.subject |
Binding Sites |
eng |
dc.subject |
Coenzymes |
eng |
dc.subject.ddc |
570 | Biowissenschaften, Biologie
|
|
dc.subject.ddc |
540 | Chemie
|
|
dc.title |
The periplasmic transaminase PtaA of Pseudomonas fluorescens converts the glutamic acid residue at the pyoverdine fluorophore to -ketoglutaric acid |
eng |
dc.type |
Article |
|
dc.type |
Text |
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dc.relation.essn |
1083-351X |
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dc.relation.issn |
0021-9258 |
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dc.relation.doi |
https://doi.org/10.1074/jbc.m117.812545 |
|
dc.bibliographicCitation.issue |
45 |
|
dc.bibliographicCitation.volume |
292 |
|
dc.bibliographicCitation.firstPage |
18660 |
|
dc.bibliographicCitation.lastPage |
18671 |
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dc.description.version |
publishedVersion |
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tib.accessRights |
frei zug�nglich |
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