The plant pathogen enzyme AldC is a long-chain aliphatic aldehyde dehydrogenase
| Autor: | Vinay Penna, Kate Harline, Hui-Yuan S. Chen, Joy J. Lin, Caroline M. Focht, Matthew C. Leong, Shwetha Sudhakar, Barrie Cascella, Amanda R. Groziak, Sheri A. McClerkin, Albert F. Mo, Brian R. Cox, Cynthia K. Holland, Wilhelm Cruz, Regina Liu, Chris D. Raciti, Soon Goo Lee, Barbara N. Kunkel, Sakirat O. Akadri, Joanna E. Luo, Orchid Abar, Michael Duan, Abhinav Srinath, Christine M. Meyer, Joseph D. Tang, Jesse Kao, Seong Ho Pahng, Alexander G. Bastian, Jagdeesh S. Kottapalli, Joseph M. Jez |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Pseudomonas syringae Aldehyde dehydrogenase Dehydrogenase Crystallography X-Ray Biochemistry 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins Binding site Molecular Biology Plant Diseases chemistry.chemical_classification 030102 biochemistry & molecular biology biology Chemistry Active site Cell Biology Aldehyde Dehydrogenase Enzyme structure 030104 developmental biology Octanal Enzyme Enzymology biology.protein NAD+ kinase |
| Zdroj: | J Biol Chem |
| ISSN: | 0021-9258 |
| Popis: | 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 PtoDC3000 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 PtoDC3000. 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|