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  Structures of an unusual 3-hydroxyacyl dehydratase (FabZ) from a ladderane-producing organism with an unexpected substrate preference

Dietl, A., Wellach, K., Mahadevan, P., Mertes, N., Winter, S. L., Kutsch, T., et al. (2023). Structures of an unusual 3-hydroxyacyl dehydratase (FabZ) from a ladderane-producing organism with an unexpected substrate preference. The Journal of Biological Chemistry, 299(5): 104602, pp. 1-15. doi:10.1016/j.jbc.2023.104602.

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 Urheber:
Dietl, Andreas1, Autor           
Wellach, Kathrin1, Autor           
Mahadevan, Pavithra1, Autor           
Mertes, Nicole1, Autor           
Winter, Sophie L.1, Autor           
Kutsch, Tobias1, Autor           
Walz, Carlo1, Autor           
Schlichting, Ilme1, Autor           
Fabritz, Sebastian2, Autor           
Barends, Thomas R. M.1, Autor           
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
2Chemical Biology, Max Planck Institute for Medical Research, Max Planck Society, ou_2364732              

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Schlagwörter: acyl carrier protein; enzyme catalysis; enzyme kinetics; enzyme structure; fatty acid synthase; lipid
 Zusammenfassung: The genomes of anaerobic ammonium-oxidizing (anammox) bacteria contain a gene cluster comprising genes of unusual fatty acid biosynthesis enzymes that were suggested to be involved in the synthesis of the unique "ladderane" lipids produced by these organisms. This cluster encodes an acyl carrier protein (denoted as "amxACP") and a variant of FabZ, an ACP-3-hydroxyacyl dehydratase. In this study, we characterize this enzyme, which we call anammox-specific FabZ ("amxFabZ"), to investigate the unresolved biosynthetic pathway of ladderane lipids. We find that amxFabZ displays distinct sequence differences to "canonical" FabZ, such as a bulky, apolar residue on the inside of the substrate binding tunnel, where the canonical enzyme has a glycine. Additionally, substrate screens suggest that amxFabZ efficiently converts substrates with acyl chain lengths of up to eight carbons, whereas longer substrates are converted much more slowly under the conditions used. We also present crystal structures of amxFabZs, mutational studies and the structure of a complex between amxFabZ and amxACP, which show that the structures alone cannot explain the apparent differences from canonical FabZ. Moreover, we find that while amxFabZ does dehydrate substrates bound to amxACP, it does not convert substrates bound to canonical ACP of the same anammox organism. We discuss the possible functional relevance of these observations in the light of proposals for the mechanism for ladderane biosynthesis.

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Sprache(n): eng - English
 Datum: 2023-03-072022-05-232023-03-082023-03-112023-05
 Publikationsstatus: Erschienen
 Seiten: 15
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Art des Abschluß: -

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Titel: The Journal of Biological Chemistry
  Andere : JBC
  Kurztitel : J. Biol. Chem.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Seiten: - Band / Heft: 299 (5) Artikelnummer: 104602 Start- / Endseite: 1 - 15 Identifikator: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1