ArticleBiochemistry2015
Structural Basis of Substrate Recognition by Aldehyde Dehydrogenase 7A1.
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Targeting ALDH7A1 with covalent inhibitors reveals new chemical space for prostate cancer therapy.Journal of enzyme inhibition and medicinal chemistry · 2026Article
- StoPred: Accurate Stoichiometry Prediction for Protein Complexes Using Protein Language Models and Graph Attention.Research square · 2025Article
- StoPred: Accurate Stoichiometry Prediction for Protein Complexes Using Protein Language Models and Graph Attention.bioRxiv : the preprint server for biology · 2025Article
- Rapid and accurate prediction of protein homo-oligomer symmetry using Seq2Symm.Nature communications · 2025Article
- N-carboxyacyl and N-α-aminoacyl derivatives of aminoaldehydes as shared substrates of plant aldehyde dehydrogenases 10 and 7.Amino acids · 2024Article
- Contribution of a C-Terminal Extension to the Substrate Affinity and Oligomeric Stability of Aldehyde Dehydrogenase fromBiochemistry · 2024Article
- Biochemical, structural, and computational analyses of two new clinically identified missense mutations of ALDH7A1.Chemico-biological interactions · 2024Article
- Rapid and accurate prediction of protein homo-oligomer symmetry with Seq2Symm.Research square · 2024Article
- Targeting colorectal cancer with small-molecule inhibitors of ALDH1B1.Nature chemical biology · 2022Article
- Structure of putative tumor suppressor ALDH1L1.Communications biology · 2022Article
- Modeling and Structure Determination of Homo-Oligomeric Proteins: An Overview of Challenges and Current Approaches.International journal of molecular sciences · 2021Review
- Impact of missense mutations in the ALDH7A1 gene on enzyme structure and catalytic function.Biochimie · 2021Review
- Structural analysis of prolines and hydroxyprolines binding to the l-glutamate-γ-semialdehyde dehydrogenase active site of bifunctional proline utilization A.Archives of biochemistry and biophysics · 2021Article
- Investigating the reaction and substrate preference of indole-3-acetaldehyde dehydrogenase from the plant pathogen Pseudomonas syringae PtoDC3000.Bioscience reports · 2020Article
- The plant pathogen enzyme AldC is a long-chain aliphatic aldehyde dehydrogenase.The Journal of biological chemistry · 2020Article
- Inhibition, crystal structures, and in-solution oligomeric structure of aldehyde dehydrogenase 9A1.Archives of biochemistry and biophysics · 2020Article
- Highlighting Human Enzymes Active in Different Metabolic Pathways and Diseases: The Case Study of EC 1.2.3.1 and EC 2.3.1.9.Biomedicines · 2020Article
- Structural analysis of pathogenic mutations targeting Glu427 of ALDH7A1, the hot spot residue of pyridoxine-dependent epilepsy.Journal of inherited metabolic disease · 2020Article
- Structural and biochemical consequences of pyridoxine-dependent epilepsy mutations that target the aldehyde binding site of aldehyde dehydrogenase ALDH7A1.The FEBS journal · 2020Article
- Structural Biology of Proline Catabolic Enzymes.Antioxidants & redox signaling · 2019Review
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2 authors.
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Abstract
Aldehyde dehydrogenase 7A1 (ALDH7A1) is part of lysine catabolism and catalyzes the NAD(+)-dependent oxidation of α-aminoadipate semialdehyde to α-aminoadipate. Herein, we describe a structural study of human ALDH7A1 focused on substrate recognition. Five crystal structures and small-angle X-ray scattering data are reported, including the first crystal structure of any ALDH7 family member complexed with α-aminoadipate. The product binds with the ε-carboxylate in the oxyanion hole, the aliphatic chain packed into an aromatic box, and the distal end of the product anchored by electrostatic interactions with five conserved residues. This binding mode resembles that of glutamate bound to the proline catabolic enzyme ALDH4A1. Analysis of ALDH7A1 and ALDH4A1 structures suggests key interactions that underlie substrate discrimination. Structures of apo ALDH7A1 reveal dramatic conformational differences from the product complex. Product binding is associated with a 16 Å movement of the C-terminus into the active site, which stabilizes the active conformation of the aldehyde substrate anchor loop. The fact that the C-terminus is part of the active site was hitherto unknown. Interestingly, the C-terminus and aldehyde anchor loop are disordered in a new tetragonal crystal form of the apoenzyme, implying that these parts of the enzyme are highly flexible. Our results suggest that the active site of ALDH7A1 is disassembled when the aldehyde site is vacant, and the C-terminus is a mobile element that forms quaternary structural interactions that aid aldehyde binding. These results are relevant to the c.1512delG genetic deletion associated with pyridoxine-dependent epilepsy, which alters the C-terminus of ALDH7A1.
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