Unknown

Dataset Information

0

Bimodular peptide synthetase SidE produces fumarylalanine in the human pathogen Aspergillus fumigatus.


ABSTRACT: The filamentous mold Aspergillus fumigatus causes invasive aspergillosis, a potentially life-threatening infectious disease, in humans. The sidE gene encodes a bimodular peptide synthetase and was shown previously to be strongly upregulated during initiation of murine lung infection. In this study, we characterized the two adenylation domains of SidE with the ATP-[(32)P]pyrophosphate exchange assay in vitro, which identified fumarate and l-alanine, respectively, as the preferred substrates. Using full-length holo-SidE, fumarylalanine (FA) formation was observed in vitro. Furthermore, FA was identified in A. fumigatus culture supernatants under inducing conditions, unless sidE was genetically inactivated. As FA is structurally related to established pharmaceutical products exerting immunomodulatory activity, this work may contribute to our understanding of the virulence of A. fumigatus.

SUBMITTER: Steinchen W 

PROVIDER: S-EPMC3811484 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications

Bimodular peptide synthetase SidE produces fumarylalanine in the human pathogen Aspergillus fumigatus.

Steinchen Wieland W   Lackner Gerald G   Yasmin Sabiha S   Schrettl Markus M   Dahse Hans-Martin HM   Haas Hubertus H   Hoffmeister Dirk D  

Applied and environmental microbiology 20130823 21


The filamentous mold Aspergillus fumigatus causes invasive aspergillosis, a potentially life-threatening infectious disease, in humans. The sidE gene encodes a bimodular peptide synthetase and was shown previously to be strongly upregulated during initiation of murine lung infection. In this study, we characterized the two adenylation domains of SidE with the ATP-[(32)P]pyrophosphate exchange assay in vitro, which identified fumarate and l-alanine, respectively, as the preferred substrates. Usin  ...[more]

Similar Datasets

| S-EPMC1489275 | biostudies-literature
| S-EPMC3187245 | biostudies-literature
| S-EPMC6013660 | biostudies-literature
| S-EPMC3590312 | biostudies-literature
| S-EPMC3346476 | biostudies-literature
| S-EPMC3728708 | biostudies-literature
| S-EPMC8782537 | biostudies-literature
| S-EPMC3255943 | biostudies-literature
| S-EPMC4063936 | biostudies-literature
| S-EPMC8496221 | biostudies-literature