ArticleProtein science : a publication of the Protein Society2004
Structure of human brain fructose 1,6-(bis)phosphate aldolase: linking isozyme structure with function.
Article in Protein science : a publication of the Protein Society, 2004. 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, 68 citations in OpenAlex.
- The multifaceted roles of aldolase A in cancer: glycolysis, cytoskeleton, translation and beyond.Human cell · 2025Review
- Identification of positions in human aldolase a that are neutral for apparent KArchives of biochemistry and biophysics · 2024Article
- Proteomic analysis of Rana sylvatica reveals differentially expressed proteins in liver in response to anoxia, dehydration or freezing stress.Scientific reports · 2024Article
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- Newborns with Favourable Outcomes after Perinatal Asphyxia Have Upregulated Glucose Metabolism-Related Proteins in Plasma.Biomolecules · 2023Article
- The Network Basis for the Structural Thermostability and the Functional Thermoactivity of Aldolase B.Molecules (Basel, Switzerland) · 2023Article
- Comparative Proteomic Analysis of Liver Tissues and Serum inInternational journal of molecular sciences · 2022Article
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- Neurodegenerative and functional signatures of the cerebellar cortex in m.3243A > G patients.Brain communications · 2022Article
- Integrated proteogenomic analysis revealed the metabolic heterogeneity in noncancerous liver tissues of patients with hepatocellular carcinoma.Journal of hematology & oncology · 2021Article
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- Proteomics analysis of protein biomarkers inJournal of traditional and complementary medicine · 2021Article
- Transcriptomic Responses Induced in Muscle and Adipose Tissues of Growing Pigs by Intravenous Infusion of Sodium Butyrate.Biology · 2021Article
- Multifunctional Fructose 1,6-Bisphosphate Aldolase as a Therapeutic Target.Frontiers in molecular biosciences · 2021Review
- The Relationship Between Zebrin Expression and Cerebellar Functions: Insights From Neuroimaging Studies.Frontiers in neurology · 2020Review
- Optimization of the Turnover in Artificial Enzymes via Directed Evolution Results in the Coupling of Protein Dynamics to Chemistry.Journal of the American Chemical Society · 2019Article
- Article
- Neural Stem Cell Death Mechanisms Induced by Amyloid Beta.Dementia and neurocognitive disorders · 2017Article
- The Cerebellum: Adaptive Prediction for Movement and Cognition.Trends in cognitive sciences · 2017Review
- High Expression of Aldolase B Confers a Poor Prognosis for Rectal Cancer Patients Receiving Neoadjuvant Chemoradiotherapy.Journal of Cancer · 2017Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Fructose-1,6-(bis)phosphate aldolase is a ubiquitous enzyme that catalyzes the reversible aldol cleavage of fructose-1,6-(bis)phosphate and fructose 1-phosphate to dihydroxyacetone phosphate and either glyceral-dehyde-3-phosphate or glyceraldehyde, respectively. Vertebrate aldolases exist as three isozymes with different tissue distributions and kinetics: aldolase A (muscle and red blood cell), aldolase B (liver, kidney, and small intestine), and aldolase C (brain and neuronal tissue). The structures of human aldolases A and B are known and herein we report the first structure of the human aldolase C, solved by X-ray crystallography at 3.0 A resolution. Structural differences between the isozymes were expected to account for isozyme-specific activity. However, the structures of isozymes A, B, and C are the same in their overall fold and active site structure. The subtle changes observed in active site residues Arg42, Lys146, and Arg303 are insufficient to completely account for the tissue-specific isozymic differences. Consequently, the structural analysis has been extended to the isozyme-specific residues (ISRs), those residues conserved among paralogs. A complete analysis of the ISRs in the context of this structure demonstrates that in several cases an amino acid residue that is conserved among aldolase C orthologs prevents an interaction that occurs in paralogs. In addition, the structure confirms the clustering of ISRs into discrete patches on the surface and reveals the existence in aldolase C of a patch of electronegative residues localized near the C terminus. Together, these structural changes highlight the differences required for the tissue and kinetic specificity among aldolase isozymes.
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