The plant pathogen enzyme AldC is a long-chain aliphatic aldehyde dehydrogenase.

Autor:	Lee SG; Department of Biology, Washington University in St. Louis, St. Louis, Missouri, USA; Department of Chemistry and Biochemistry, University of North Carolina-Wilmington, Wilmington, North Carolina, USA., Harline K; Department of Biology, Washington University in St. Louis, St. Louis, Missouri, USA., Abar O; Department of Biology, Washington University in St. Louis, St. Louis, Missouri, USA., Akadri SO; Department of Biology, Washington University in St. Louis, St. Louis, Missouri, USA., Bastian AG; Department of Biology, Washington University in St. Louis, St. Louis, Missouri, USA., Chen HS; Department of Biology, Washington University in St. Louis, St. Louis, Missouri, USA., Duan M; Department of Biology, Washington University in St. Louis, St. Louis, Missouri, USA., Focht CM; Department of Biology, Washington University in St. Louis, St. Louis, Missouri, USA., Groziak AR; Department of Biology, Washington University in St. Louis, St. Louis, Missouri, USA., Kao J; Department of Biology, Washington University in St. Louis, St. Louis, Missouri, USA., Kottapalli JS; Department of Biology, Washington University in St. Louis, St. Louis, Missouri, USA., Leong MC; Department of Biology, Washington University in St. Louis, St. Louis, Missouri, USA., Lin JJ; Department of Biology, Washington University in St. Louis, St. Louis, Missouri, USA., Liu R; Department of Biology, Washington University in St. Louis, St. Louis, Missouri, USA., Luo JE; Department of Biology, Washington University in St. Louis, St. Louis, Missouri, USA., Meyer CM; Department of Biology, Washington University in St. Louis, St. Louis, Missouri, USA., Mo AF; Department of Biology, Washington University in St. Louis, St. Louis, Missouri, USA., Pahng SH; Department of Biology, Washington University in St. Louis, St. Louis, Missouri, USA., Penna V; Department of Biology, Washington University in St. Louis, St. Louis, Missouri, USA., Raciti CD; Department of Biology, Washington University in St. Louis, St. Louis, Missouri, USA., Srinath A; Department of Biology, Washington University in St. Louis, St. Louis, Missouri, USA., Sudhakar S; Department of Biology, Washington University in St. Louis, St. Louis, Missouri, USA., Tang JD; Department of Biology, Washington University in St. Louis, St. Louis, Missouri, USA., Cox BR; Department of Chemistry and Biochemistry, University of North Carolina-Wilmington, Wilmington, North Carolina, USA., Holland CK; Department of Biology, Washington University in St. Louis, St. Louis, Missouri, USA; Department of Biology, Williams College, Williamstown, Massachusetts, USA., Cascella B; Department of Biology, Washington University in St. Louis, St. Louis, Missouri, USA., Cruz W; Department of Biology, Washington University in St. Louis, St. Louis, Missouri, USA., McClerkin SA; Department of Biology, Washington University in St. Louis, St. Louis, Missouri, USA; Department of Molecular Genetics and Cell Biology, University of Chicago, Chicago, Illinois, USA., Kunkel BN; Department of Biology, Washington University in St. Louis, St. Louis, Missouri, USA., Jez JM; Department of Biology, Washington University in St. Louis, St. Louis, Missouri, USA. Electronic address: jjez@wustl.edu.
Jazyk:	angličtina
Zdroj:	The Journal of biological chemistry [J Biol Chem] 2020 Oct 02; Vol. 295 (40), pp. 13914-13926. Date of Electronic Publication: 2020 Aug 12.
DOI:	10.1074/jbc.RA120.014747
Abstrakt:	Aldehyde dehydrogenases are versatile enzymes that serve a range of biochemical functions. Although traditionally considered metabolic housekeeping enzymes because of their ability to detoxify reactive aldehydes, like those generated from lipid peroxidation damage, the contributions of these enzymes to other biological processes are widespread. For example, the plant pathogen Pseudomonas syringae strain Pto DC3000 uses an indole-3-acetaldehyde dehydrogenase to synthesize the phytohormone indole-3-acetic acid to elude host responses. Here we investigate the biochemical function of AldC from Pto DC3000. Analysis of the substrate profile of AldC suggests that this enzyme functions as a long-chain aliphatic aldehyde dehydrogenase. The 2.5 Å resolution X-ray crystal of the AldC C291A mutant in a dead-end complex with octanal and NAD + reveals an apolar binding site primed for aliphatic aldehyde substrate recognition. Functional characterization of site-directed mutants targeting the substrate- and NAD(H)-binding sites identifies key residues in the active site for ligand interactions, including those in the "aromatic box" that define the aldehyde-binding site. Overall, this study provides molecular insight for understanding the evolution of the prokaryotic aldehyde dehydrogenase superfamily and their diversity of function. Competing Interests: Conflict of interest—The authors declare that they have no conflicts of interest with the contents of this article. (© 2020 Lee et al.)
Databáze:	MEDLINE
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