ArticleBiochemistry2008
Examination of the mechanism of human brain aspartoacylase through the binding of an intermediate analogue.
Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 43 citations in OpenAlex.
- Article
- Deep mutational scanning reveals a correlation between degradation and toxicity of thousands of aspartoacylase variants.Nature communications · 2024Article
- Cellular and molecular mechanisms of aspartoacylase and its role in Canavan disease.Cell & bioscience · 2024Review
- Mapping the degradation pathway of a disease-linked aspartoacylase variant.PLoS genetics · 2021Article
- Degradation of the microbial stress protectants and chemical chaperones ectoine and hydroxyectoine by a bacterial hydrolase-deacetylase complex.The Journal of biological chemistry · 2020Article
- Comparative computational assessment of the pathogenicity of mutations in the Aspartoacylase enzyme.Metabolic brain disease · 2017Article
- Clinically Distinct Phenotypes of Canavan Disease Correlate with Residual Aspartoacylase Enzyme Activity.Human mutation · 2017Article
- Two patients with Canavan disease and structural modeling of a novel mutation.Metabolic brain disease · 2017Article
- Structural modeling of p.V31F variant in the aspartoacylase gene.Metabolic brain disease · 2016Article
- Enhanced brain distribution of modified aspartoacylase.Molecular genetics and metabolism · 2014Article
- Relationship between enzyme properties and disease progression in Canavan disease.Journal of inherited metabolic disease · 2013Article
- A blueprint of ectoine metabolism from the genome of the industrial producer Halomonas elongata DSM 2581 T.Environmental microbiology · 2011Article
- Modification of aspartoacylase for potential use in enzyme replacement therapy for the treatment of Canavan disease.Molecular genetics and metabolism · 2011Article
- Structures of aminoacylase 3 in complex with acetylated substrates.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Are astrocytes the missing link between lack of brain aspartoacylase activity and the spongiform leukodystrophy in Canavan disease?Neurochemical research · 2009Article
- Mouse aminoacylase 3: a metalloenzyme activated by cobalt and nickel.Biochimica et biophysica acta · 2009Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Canavan disease is a fatal neurological disorder caused by the malfunctioning of a single metabolic enzyme, aspartoacylase, that catalyzes the deacetylation of N-acetyl-L-aspartate to produce L-aspartate and acetate. The structure of human brain aspartoacylase has been determined in complex with a stable tetrahedral intermediate analogue, N-phosphonomethyl-L-aspartate. This potent inhibitor forms multiple interactions between each of its heteroatoms and the substrate binding groups arrayed within the active site. The binding of the catalytic intermediate analogue induces the conformational ordering of several substrate binding groups, thereby setting up the active site for catalysis. The highly ordered binding of this inhibitor has allowed assignments to be made for substrate binding groups and provides strong support for a carboxypeptidase-type mechanism for the hydrolysis of the amide bond of the substrate, N-acetyl- l-aspartate.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.