ALDOB encodes liver-type fructose-bisphosphate aldolase, a cytosolic class I aldolase expressed prominently in liver, kidney and intestine. Its homotetramer catalyzes reversible cleavage of fructose 1,6-bisphosphate into dihydroxyacetone phosphate and glyceraldehyde 3-phosphate, contributing to glycolysis and the reverse gluconeogenic reaction. The same enzyme efficiently cleaves fructose 1-phosphate into dihydroxyacetone phosphate and glyceraldehyde during dietary fructose catabolism. Biallelic loss of function causes hereditary fructose intolerance. In addition to these catalytic roles, ALDOB has experimentally supported interactions with the cytoskeleton and V-ATPase, and a reported noncatalytic scaffold activity that strengthens p53-mediated G6PD inhibition in hepatocellular carcinoma models.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004332 fructose-bisphosphate aldolase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Retain conserved fructose-bisphosphate aldolase catalysis. Reason: The seeded IBA names ancestral node PTN000179343. The current cached PTHR11627 PAINT export instead places this reaction at PTN004279385, with human experimental descendants; the historical node correspondence was not reconstructed. Direct purified human ALDOB kinetics independently establish cleavage of fructose 1,6-bisphosphate (PMID:10625657; PMID:10970798), so the biological assertion is accepted without alleging loss or erroneous phylogenetic placement. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000179343 UNRESOLVED This is the preserved GOA ancestor. The current cached PTHR11627 export lists the corresponding term at PTN004279385 instead; historical node reconciliation and the full tree/MSA were not reconstructed. Independent human evidence supports the annotation, and no lineage-specific loss is inferred. Supporting Evidence: PMID:10625657 We describe the biochemical and biophysical characterization of seven natural human aldolase B variants, identified in patients suffering from hereditary fructose intolerance and expressed as recombinant proteins in E. coli, from which they were purified to homogeneity. PMID:10970798 The catalytic efficiency of protein Gln(303) is approx. 1/100 that of the wild-type for substrates fructose 1,6-bisphosphate and fructose 1-phosphate. |
| GO:0005829 cytosol | IBA GO_REF:0000033 | ACCEPT | Summary: The inherited cytosolic location agrees with ALDOB metabolism. Reason: The IBA cytosolic compartment agrees with independent human enzyme/pathway evidence and the curated cytosolic reaction (Reactome:R-HSA-71496). The current PAINT export uses PTN004279385 for this location rather than the seeded PTN000179343; that version difference is recorded as a provenance limit, not evidence of a biological relocation. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000179343 UNRESOLVED This is the preserved GOA ancestor. The current cached PTHR11627 export lists the corresponding term at PTN004279385 instead; historical node reconciliation and the full tree/MSA were not reconstructed. Independent human evidence supports the annotation, and no lineage-specific loss is inferred. Supporting Evidence: Reactome:R-HSA-71496 Cytosolic aldolase catalyzes the cleavage of D-fructose 1,6-bisphosphate to yield dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate. |
| GO:0006096 glycolytic process | IBA GO_REF:0000033 | ACCEPT | Summary: ALDOB directly performs the aldol-cleavage step of glycolysis. Reason: Human ALDOB cleaves fructose 1,6-bisphosphate into the two triose phosphates, directly executing a glycolytic reaction. The PAINT family assertion is corroborated by human enzymology (PMID:10625657; PMID:10970798); target experimental evidence among ancestral descendants is legitimate grounding rather than circularity. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000179343 UNRESOLVED This is the preserved GOA ancestor. The current cached PTHR11627 export lists the corresponding term at PTN004279385 instead; historical node reconciliation and the full tree/MSA were not reconstructed. Independent human evidence supports the annotation, and no lineage-specific loss is inferred. Supporting Evidence: PMID:10625657 Fructaldolases (EC 4.1.2.13) are ancient enzymes of glycolysis that catalyze the reversible cleavage of phosphofructose esters into cognate triose (phosphates). PMID:10625657 We describe the biochemical and biophysical characterization of seven natural human aldolase B variants, identified in patients suffering from hereditary fructose intolerance and expressed as recombinant proteins in E. coli, from which they were purified to homogeneity. |
| GO:0030388 fructose 1,6-bisphosphate metabolic process | IBA GO_REF:0000033 | ACCEPT | Summary: ALDOB directly metabolizes fructose 1,6-bisphosphate. Reason: Purified human ALDOB acts on fructose 1,6-bisphosphate, and the reversible reaction also produces it during gluconeogenesis. This substrate-level process accurately covers the enzyme chemistry; the inherited PAINT assertion does not depend on an indirect phenotype. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000179343 UNRESOLVED This is the preserved GOA ancestor. The current cached PTHR11627 export lists the corresponding term at PTN004279385 instead; historical node reconciliation and the full tree/MSA were not reconstructed. Independent human evidence supports the annotation, and no lineage-specific loss is inferred. Supporting Evidence: PMID:10970798 The catalytic efficiency of protein Gln(303) is approx. 1/100 that of the wild-type for substrates fructose 1,6-bisphosphate and fructose 1-phosphate. Reactome:R-HSA-71495 In this freely reversible cytosolic reaction, DHAP (dihydroxyacetone phosphate) and GA3P (D-glyceraldehyde 3-phosphate) react to form F1,6PP (D-fructose 1,6-bisphosphate). |
| GO:0061609 fructose-1-phosphate aldolase activity | IBA GO_REF:0000033 | ACCEPT | Summary: The ALDOB-lineage ancestral fructose-1-phosphate reaction is supported. Reason: Cached PAINT places GO:0061609 at PTN002614886, grounded in human P05062 and mouse Aldob MGI:87995. Direct human activity with fructose 1-phosphate confirms inheritance of this substrate specificity. The target appearing among the descendants is valid experimental grounding. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002614886 SUPPORTS TRANSFER The cached IBD explicitly carries GO:0061609 with human P05062 and mouse MGI:87995 descendants. Direct human kinetics support the target; the whole ancestral MSA was not reanalyzed. Supporting Evidence: PMID:10970798 The catalytic efficiency of protein Gln(303) is approx. 1/100 that of the wild-type for substrates fructose 1,6-bisphosphate and fructose 1-phosphate. PMID:2649152 Enzymatically active forms of human aldolase have been generated in the cells when transfected with either pHAA47, a human aldolase A expression plasmid, or pHAB 141, a human aldolase B expression plasmid. |
| GO:0004332 fructose-bisphosphate aldolase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Combined mappings identify the established bisphosphate aldolase reaction. Reason: The cached human UniProt reaction is RHEA:14729/EC:4.1.2.13. GOA additionally supplies the FBA-I InterPro domain and mouse Aldob ortholog sources. These agree with purified human catalytic measurements; a domain match alone would not establish the separate fructose-1-phosphate specificity. Propagation Review Root cause: NO FAILURE CORE Sources checked: RHEA:14729 SUPPORTS TRANSFER Cached human UniProt explicitly assigns the bisphosphate cleavage reaction; direct human kinetics corroborate the chemistry. EC:4.1.2.13 SUPPORTS TRANSFER Cached human UniProt explicitly assigns the bisphosphate cleavage reaction; direct human kinetics corroborate the chemistry. InterPro:IPR000741 UNRESOLVED The FBA-I domain mapping is present in GOA; its current mapping predicates were not independently inspected. UniProtKB:Q91Y97 SUPPORTS TRANSFER Mouse Aldob is the ortholog; MGI traces experimental activity to the Aldob knockout study PMID:25637246. Its physiological evidence is supplemented by direct human kinetics. ensembl:ENSMUSP00000029987 SUPPORTS TRANSFER The Ensembl source is the mouse Aldob protein paired with Q91Y97 in GOA, not a separate experimental measurement. Supporting Evidence: PMID:10970798 The catalytic efficiency of protein Gln(303) is approx. 1/100 that of the wild-type for substrates fructose 1,6-bisphosphate and fructose 1-phosphate. PMID:10625657 We describe the biochemical and biophysical characterization of seven natural human aldolase B variants, identified in patients suffering from hereditary fructose intolerance and expressed as recombinant proteins in E. coli, from which they were purified to homogeneity. |
| GO:0005829 cytosol | IEA GO_REF:0000120 | ACCEPT | Summary: Retain cytosol from ortholog and compartment mappings. Reason: The mouse Aldob and UniProt cytosol mappings agree with the human cytosolic aldolase reaction. The individual historical mouse location experiment was not recovered, but independent human location/pathway evidence supports the transferred broad compartment. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:Q91Y97 UNRESOLVED Mouse Aldob identity is verified, but the exact experimental source underlying this historical cytosolic transfer was not reconstructed. Human cytosolic evidence independently supports acceptance. ensembl:ENSMUSP00000029987 SUPPORTS TRANSFER GOA links this protein to mouse Aldob Q91Y97; it supplies ortholog identity, not an independent localization assay. UniProtKB-SubCell:SL-0091 SUPPORTS TRANSFER The cytosol vocabulary mapping agrees with the preserved human UniProt compartment and cytosolic reaction. Supporting Evidence: Reactome:R-HSA-71496 Cytosolic aldolase catalyzes the cleavage of D-fructose 1,6-bisphosphate to yield dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate. |
| GO:0006096 glycolytic process | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic pathway mappings agree with ALDOB glycolytic participation. Reason: ALDOB directly catalyzes a glycolytic step. UniPathway:UPA00109 and the FBA-I mapping are consistent with that measured reaction. The ARBA predicate set was not inspected, so rule internals are not treated as independently validated evidence. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00035055 UNRESOLVED ARBA:ARBA00035055 was not found in the local rules/arba/rules_data.json summary; complete rule predicates and training annotations remain uninspected. Independent human substrate chemistry supports the target judgment. InterPro:IPR000741 UNRESOLVED Current domain-to-process mapping internals were not inspected; human catalytic evidence independently supports glycolysis. UniPathway:UPA00109 SUPPORTS TRANSFER The preserved UniProt pathway record links this identifier to glycolysis, consistent with the ALDOB reaction. Supporting Evidence: PMID:10625657 Fructaldolases (EC 4.1.2.13) are ancient enzymes of glycolysis that catalyze the reversible cleavage of phosphofructose esters into cognate triose (phosphates). PMID:10625657 We describe the biochemical and biophysical characterization of seven natural human aldolase B variants, identified in patients suffering from hereditary fructose intolerance and expressed as recombinant proteins in E. coli, from which they were purified to homogeneity. |
| GO:0030388 fructose 1,6-bisphosphate metabolic process | IEA GO_REF:0000117 | ACCEPT | Summary: The electronic substrate-process assignment matches measured turnover. Reason: Direct human fructose 1,6-bisphosphate turnover supports this process independently of ARBA:ARBA00087539. Acceptance of the biological assertion does not imply that the rule training evidence or predicates were recovered. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00087539 UNRESOLVED The local rules/arba/rules_data.json summary was inspected. It lists 3 condition set(s), condition types taxon, FunFam id, and 3.40.50.460:FF:000001 (ATP-dependent 6-phosphofructokinase), 3.40.190.80:FF:000001 (Fructose-1,6-bisphosphatase class 1), 3.20.20.70:FF:000021 (Fructose-bisphosphate aldolase), 3.40.50.450:FF:000043 (ATP-dependent 6-phosphofructokinase, platelet type). The summary does not expose complete grouped taxon predicates, training annotations or a target match, so exact derivation remains unresolved. The target judgment follows independent human biology and the GO ligand/process definition. Supporting Evidence: PMID:10970798 The catalytic efficiency of protein Gln(303) is approx. 1/100 that of the wild-type for substrates fructose 1,6-bisphosphate and fructose 1-phosphate. |
| GO:0034451 centriolar satellite | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Retain the reported peripheral centrosomal pool as non-core. Reason: The UniProt centriolar-satellite vocabulary derives from the BBS interaction/localization study PMID:18000879. Its full text describes overexpressed EGFP-ALDOB in HeLa cells near, rather than overlapping, gamma-tubulin, with a possible partial satellite distribution. Retain the curator-level compartment inference as non-core without asserting an established endogenous hepatic ciliary function. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB-SubCell:SL-0485 SUPPORTS TRANSFER The human UniProt centriolar-satellite location traces to PMID:18000879; the full study supports a tentative peripheral centrosomal distribution in transfected HeLa cells. Supporting Evidence: |
| GO:0070061 fructose binding | IEA GO_REF:0000117 | REMOVE | Summary: Free-fructose binding is not established by phosphorylated-substrate chemistry. Reason: The live GO:0070061 definition binds the unphosphorylated ketohexose fructose. ALDOB biochemical evidence instead establishes fructose 1-phosphate and fructose 1,6-bisphosphate substrates, including the complete assays in PMID:10625657. Those distinct ligands do not justify free-fructose binding. Remove this unsupported electronic assignment without claiming that an untested free-fructose interaction is chemically impossible; the exact ARBA derivation remains unresolved. Propagation Review Root cause: TERM SCOPING PROBLEM Sources checked: ARBA:ARBA00092505 UNRESOLVED The local rules/arba/rules_data.json summary was inspected. It lists 1 condition set(s), condition types taxon, FunFam id, and 3.20.20.70:FF:000021 (Fructose-bisphosphate aldolase). The summary does not expose complete grouped taxon predicates, training annotations or a target match, so exact derivation remains unresolved. The target judgment follows independent human biology and the GO ligand/process definition. Supporting Evidence: PMID:10625657 We describe the biochemical and biophysical characterization of seven natural human aldolase B variants, identified in patients suffering from hereditary fructose intolerance and expressed as recombinant proteins in E. coli, from which they were purified to homogeneity. PMID:10970798 The catalytic efficiency of protein Gln(303) is approx. 1/100 that of the wild-type for substrates fructose 1,6-bisphosphate and fructose 1-phosphate. |
| GO:0005515 protein binding | IPI PMID:18000879 Novel interaction partners of Bardet-Biedl syndrome proteins... | REMOVE | Summary: The BBS interactions do not identify a specific ALDOB molecular activity. Reason: PMID:18000879 positively supports Y2H/coimmunoprecipitation and colocalization of ALDOB with BBS proteins. The mapped partners are BBS1, BBS2, BBS4 and BBS7. These findings do not by themselves establish adaptor catalysis or another specific MF; remove the uninformative generic binding term while preserving the positive interaction and localization evidence in the source assessment. Supporting Evidence: PMID:18000879 Protein interactions were supported by coimmunoprecipitation analyses (ALDOB, EPAS1) and substantiated by colocalization studies at the subcellular level (ALDOB, EXOC7, FLOT1, KRT18, PAX2). |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: Remove generic binding while retaining the ALDOA interaction provenance. Reason: GOA identifies ALDOA/P04075 as the partner in the human liver Y2H network PMID:21988832. The pair does not establish homomeric binding of identical ALDOB subunits, and no more specific functional interaction was resolved here. Remove the uninformative MF, without denying the interaction. PMID:29254952 corrects only an author name and does not invalidate the network. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: BioPlex association with ALDOA does not supply a specific ALDOB MF. Reason: The source is the BioPlex affinity-purification network PMID:33961781 and the mapped partner is ALDOA/P04075. The cached extraction does not expose the pair-level supplement, and association cannot be promoted to a functional heterotetramer claim. Generic protein binding is removed as uninformative, without treating the interaction as false or relabeling it as identical-protein binding. |
| GO:0006001 fructose catabolic process | IEA GO_REF:0000107 | ACCEPT | Summary: Mouse-to-human fructose catabolism is supported by conserved chemistry. Reason: The proximate donor is mouse Aldob Q91Y97. The historical MGI comparative graph traces fructose-catabolism evidence to PMID:29533924 (IMP) and PMID:4343087 (IDA). The 2018 primary mouse study follows Aldob deficiency, fructose-phosphate accumulation and upstream Khk interventions; the older paper body was not recovered. Human ALDOB directly cleaves the phosphorylated fructose intermediate, independently establishing participation in this pathway. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:Q91Y97 SUPPORTS TRANSFER Mouse Aldob has experimentally curated fructose-catabolism provenance (PMID:29533924 and PMID:4343087 in the MGI graph generated 2023-03-10). The 2018 primary study was read; the older assay remains unresolved. Direct human F1P cleavage independently supports transfer. ensembl:ENSMUSP00000029987 SUPPORTS TRANSFER The GOA protein identifier is the mouse Aldob ortholog associated with Q91Y97. Supporting Evidence: PMID:3383242 Hereditary fructose intolerance (HFI) is a human autosomal recessive disease caused by a deficiency of aldolase B that results in an inability to metabolize fructose and related sugars. PMID:10970798 The catalytic efficiency of protein Gln(303) is approx. 1/100 that of the wild-type for substrates fructose 1,6-bisphosphate and fructose 1-phosphate. |
| GO:0061609 fructose-1-phosphate aldolase activity | IEA GO_REF:0000120 | ACCEPT | Summary: The combined mapping captures ALDOB fructose-1-phosphate cleavage. Reason: The preserved human UniProt reaction RHEA:30851 is fructose 1-phosphate cleavage to glyceraldehyde and dihydroxyacetone phosphate. Mouse ortholog evidence is traceable to Aldob-deficient models (PMID:25637246), and direct human assays establish the same substrate specificity independently. Propagation Review Root cause: NO FAILURE CORE Sources checked: RHEA:30851 SUPPORTS TRANSFER The preserved human UniProt record explicitly assigns this F1P-to-glyceraldehyde/DHAP reaction. UniProtKB:Q91Y97 SUPPORTS TRANSFER Mouse MGI experimental F1P-aldolase annotations include PMID:25637246. Its knockout physiology supports the donor role; direct human recombinant assays establish target catalysis. ensembl:ENSMUSP00000029987 SUPPORTS TRANSFER GOA identifies the mouse Aldob ortholog; this is not an independent biochemical source. Supporting Evidence: PMID:2649152 Enzymatically active forms of human aldolase have been generated in the cells when transfected with either pHAA47, a human aldolase A expression plasmid, or pHAB 141, a human aldolase B expression plasmid. PMID:10970798 The catalytic efficiency of protein Gln(303) is approx. 1/100 that of the wild-type for substrates fructose 1,6-bisphosphate and fructose 1-phosphate. |
| GO:0006094 gluconeogenesis | TAS Reactome:R-HSA-70263 | ACCEPT | Summary: ALDOB performs the reversible aldol-condensation step of gluconeogenesis. Reason: Reactome:R-HSA-70263 describes the pathway, and the linked reaction R-HSA-71495 specifies cytosolic condensation of glyceraldehyde 3-phosphate and DHAP into fructose 1,6-bisphosphate. ALDOB catalyzes this step; its participation does not depend solely on hypoglycemia after fructose intoxication. Supporting Evidence: Reactome:R-HSA-71495 In this freely reversible cytosolic reaction, DHAP (dihydroxyacetone phosphate) and GA3P (D-glyceraldehyde 3-phosphate) react to form F1,6PP (D-fructose 1,6-bisphosphate). |
| GO:0061621 canonical glycolysis | TAS Reactome:R-HSA-70171 | ACCEPT | Summary: ALDOB directly contributes to canonical glycolysis. Reason: The Reactome glycolysis pathway contains the cytosolic F1,6BP-cleavage step catalyzed by aldolase tetramers. Purified human ALDOB activity supplies direct molecular grounding for this pathway-level annotation. Supporting Evidence: Reactome:R-HSA-71496 Cytosolic aldolase catalyzes the cleavage of D-fructose 1,6-bisphosphate to yield dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate. PMID:10625657 We describe the biochemical and biophysical characterization of seven natural human aldolase B variants, identified in patients suffering from hereditary fructose intolerance and expressed as recombinant proteins in E. coli, from which they were purified to homogeneity. |
| GO:0006000 fructose metabolic process | IEA GO_REF:0000120 | ACCEPT | Summary: The broader fructose-metabolism mapping accurately includes ALDOB catalysis. Reason: UniPathway:UPA00202 identifies fructose metabolism. ALDOB performs the F1P cleavage step, so this broad process is true and core at the electronic source resolution; the existing catabolic annotation provides complementary specificity. The ARBA predicates were not independently inspected. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00043337 UNRESOLVED The local rules/arba/rules_data.json summary was inspected. It lists 5 condition set(s), condition types InterPro id, taxon, FunFam id, and 1.10.287.1250:FF:000001 (Phosphotransferase), 3.40.367.20:FF:000004 (Phosphotransferase), 3.30.420.40:FF:000092 (Phosphotransferase), 3.40.1190.20:FF:000005 (Probable fructokinase-2), 3.20.20.70:FF:000021 (Fructose-bisphosphate aldolase), 3.40.1190.20:FF:000018 (Ketohexokinase). The summary does not expose complete grouped taxon predicates, training annotations or a target match, so exact derivation remains unresolved. The target judgment follows independent human biology and the GO ligand/process definition. UniPathway:UPA00202 SUPPORTS TRANSFER The preserved UniProt pathway mapping identifies fructose metabolism, matching F1P cleavage. Supporting Evidence: PMID:3383242 Hereditary fructose intolerance (HFI) is a human autosomal recessive disease caused by a deficiency of aldolase B that results in an inability to metabolize fructose and related sugars. PMID:10970798 The catalytic efficiency of protein Gln(303) is approx. 1/100 that of the wild-type for substrates fructose 1,6-bisphosphate and fructose 1-phosphate. |
| GO:0006094 gluconeogenesis | IEA GO_REF:0000041 | ACCEPT | Summary: The gluconeogenesis pathway mapping reflects a directly catalyzed reaction. Reason: UniPathway:UPA00138 agrees with ALDOB-mediated reversible formation of fructose 1,6-bisphosphate from triose phosphates. The reaction supplies positive participation evidence rather than only a perturbation effect on glucose concentrations. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniPathway:UPA00138 SUPPORTS TRANSFER The cached human UniProt pathway assignment and Reactome reverse aldol reaction support direct gluconeogenic participation. Supporting Evidence: Reactome:R-HSA-71495 In this freely reversible cytosolic reaction, DHAP (dihydroxyacetone phosphate) and GA3P (D-glyceraldehyde 3-phosphate) react to form F1,6PP (D-fructose 1,6-bisphosphate). |
| GO:0004332 fructose-bisphosphate aldolase activity | EXP PMID:6696436 Human skeletal-muscle aldolase: N-terminal sequence analysis... | UNDECIDED | Summary: The cited experimental attribution remains unresolved. Reason: The cached PMID:6696436 abstract describes sequence analysis of human skeletal-muscle aldolase. The full paper was not recovered, so an ALDOB comparison or activity experiment cannot be excluded, and the citation is not declared a wrong-paralog assignment. Human ALDOB activity is independently established, but this particular EXP source-to-gene connection remains unresolved. Supporting Evidence: PMID:10625657 We describe the biochemical and biophysical characterization of seven natural human aldolase B variants, identified in patients suffering from hereditary fructose intolerance and expressed as recombinant proteins in E. coli, from which they were purified to homogeneity. PMID:10970798 The catalytic efficiency of protein Gln(303) is approx. 1/100 that of the wild-type for substrates fructose 1,6-bisphosphate and fructose 1-phosphate. |
| GO:0070072 vacuolar proton-transporting V-type ATPase complex assembly | IMP PMID:17576770 Physical interaction between aldolase and vacuolar H+-ATPase... | KEEP AS NON CORE | Summary: Human ALDOB can support V-ATPase assembly in the tested heterologous system. Reason: The full PMID:17576770 paper tests human ALDOB A318E and R303W constructs in yeast, alongside yeast aldolase mutants. Loss of B-subunit binding disrupts assembly, whereas a catalytically deficient construct supports assembly. This is positive structural/cofactor participation, not merely a consequence of glycolytic ATP production. Retain the assembly process as non-core with its heterologous context; ALDOB is not the proton-translocating ATPase. Supporting Evidence: PMID:17576770 Functional analysis of the aldolase mutants shows that disruption of binding between aldolase and the B subunit of V-ATPase results in disassembly and malfunction of V-ATPase. |
| GO:0004332 fructose-bisphosphate aldolase activity | EXP PMID:12205126 Molecular analysis of the aldolase B gene in patients with h... | ACCEPT | Summary: Retain established human ALDOB catalysis with an unresolved source-specific assay. Reason: PMID:12205126 is the verified Spanish HFI ALDOB study, but its local record is metadata-only and accessible introductory text does not expose the original catalytic assays. Retain the curated experimental activity by deference plus independent purified human measurements (PMID:10625657; PMID:10970798), without claiming that the 2002 assay details were read. Supporting Evidence: PMID:10625657 We describe the biochemical and biophysical characterization of seven natural human aldolase B variants, identified in patients suffering from hereditary fructose intolerance and expressed as recombinant proteins in E. coli, from which they were purified to homogeneity. PMID:10970798 The catalytic efficiency of protein Gln(303) is approx. 1/100 that of the wild-type for substrates fructose 1,6-bisphosphate and fructose 1-phosphate. |
| GO:0004332 fructose-bisphosphate aldolase activity | EXP PMID:20848650 Hereditary fructose intolerance: functional study of two nov... | ACCEPT | Summary: Retain the experimentally curated bisphosphate activity. Reason: PMID:20848650 studies recombinant human ALDOB variants. The accessible abstract foregrounds altered F1P activity, while the preserved UniProt kinetic record also assigns F1,6BP measurements to this paper. The curator-supported F1,6BP activity agrees with independently measured human catalysis; no absence is inferred from the abstract emphasis. Supporting Evidence: PMID:20848650 The residual catalytic activity of the recombinant p.R46W and p.Y343H variants toward F1P was particularly altered. PMID:10970798 The catalytic efficiency of protein Gln(303) is approx. 1/100 that of the wild-type for substrates fructose 1,6-bisphosphate and fructose 1-phosphate. |
| GO:0061609 fructose-1-phosphate aldolase activity | EXP PMID:12205126 Molecular analysis of the aldolase B gene in patients with h... | ACCEPT | Summary: Retain established human ALDOB catalysis with an unresolved source-specific assay. Reason: PMID:12205126 is the verified Spanish HFI ALDOB study, but its local record is metadata-only and accessible introductory text does not expose the original catalytic assays. Retain the curated experimental activity by deference plus independent purified human measurements (PMID:10625657; PMID:10970798), without claiming that the 2002 assay details were read. Supporting Evidence: PMID:10625657 We describe the biochemical and biophysical characterization of seven natural human aldolase B variants, identified in patients suffering from hereditary fructose intolerance and expressed as recombinant proteins in E. coli, from which they were purified to homogeneity. PMID:10970798 The catalytic efficiency of protein Gln(303) is approx. 1/100 that of the wild-type for substrates fructose 1,6-bisphosphate and fructose 1-phosphate. |
| GO:0061609 fructose-1-phosphate aldolase activity | EXP PMID:20848650 Hereditary fructose intolerance: functional study of two nov... | ACCEPT | Summary: Human variant assays support fructose-1-phosphate aldolase activity. Reason: PMID:20848650 explicitly measures altered residual F1P activity of recombinant p.R46W and p.Y343H variants. This is direct human enzyme evidence; the separate clinical speculation about heterozygote susceptibility is not needed for this molecular-function judgment. Supporting Evidence: PMID:20848650 The residual catalytic activity of the recombinant p.R46W and p.Y343H variants toward F1P was particularly altered. |
| GO:0004332 fructose-bisphosphate aldolase activity | IDA PMID:35122041 Aldolase B suppresses hepatocellular carcinogenesis by inhib... | ACCEPT | Summary: Retain catalytic activity alongside the noncatalytic scaffold study. Reason: PMID:35122041 distinguishes enzyme-dependent and scaffold effects, while the individual activity-control experiments are not exposed in the accessible abstract. The existing human IDA is retained by curator deference and independent purified ALDOB kinetics. The 2025 correction PMID:41188550 replaces one Extended Data Fig. 4d image and associated source data; it does not announce withdrawal of the enzyme or scaffold conclusions. Supporting Evidence: PMID:10625657 We describe the biochemical and biophysical characterization of seven natural human aldolase B variants, identified in patients suffering from hereditary fructose intolerance and expressed as recombinant proteins in E. coli, from which they were purified to homogeneity. PMID:10970798 The catalytic efficiency of protein Gln(303) is approx. 1/100 that of the wild-type for substrates fructose 1,6-bisphosphate and fructose 1-phosphate. |
| GO:0005515 protein binding | IPI PMID:35122041 Aldolase B suppresses hepatocellular carcinogenesis by inhib... | MODIFY | Summary: Replace generic interaction with the demonstrated scaffold function. Reason: PMID:35122041 reports an ALDOB-G6PD-p53 complex in which ALDOB strengthens p53-mediated G6PD inhibition independently of aldolase catalysis. The mapped partners P11413 and P04637 are G6PD and TP53. This supports molecular adaptor activity more informatively than protein binding; the same specific MF already has its own seeded annotation. The inference is restricted to the reported hepatic/HCC setting. Proposed replacements: molecular adaptor activity Supporting Evidence: PMID:35122041 We further demonstrate that Aldob potentiates p53-mediated inhibition of G6PD in an Aldob-G6PD-p53 complex. This scaffolding effect is independent of Aldob enzymatic activity. |
| GO:0005829 cytosol | IDA PMID:35122041 Aldolase B suppresses hepatocellular carcinogenesis by inhib... | ACCEPT | Summary: Retain cytosolic ALDOB localization. Reason: The human IDA compartment annotation from PMID:35122041 agrees with ALDOB cytosolic metabolism and the independent reaction location. The accessible abstract does not show the localization image, so the IDA is retained by curator deference rather than described as a re-extracted microscopy result. Supporting Evidence: Reactome:R-HSA-71496 Cytosolic aldolase catalyzes the cleavage of D-fructose 1,6-bisphosphate to yield dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate. PMID:35122041 We further demonstrate that Aldob potentiates p53-mediated inhibition of G6PD in an Aldob-G6PD-p53 complex. This scaffolding effect is independent of Aldob enzymatic activity. |
| GO:0060090 molecular adaptor activity | IDA PMID:35122041 Aldolase B suppresses hepatocellular carcinogenesis by inhib... | KEEP AS NON CORE | Summary: Retain the reported G6PD-p53 adaptor function as context dependent. Reason: The primary abstract explicitly reports that ALDOB potentiates p53 inhibition of G6PD in a ternary complex independently of catalytic activity. This positive scaffold mechanism supports the specific MF, with a non-core designation reflecting the hepatic tumor-model context rather than uncertainty about whether an enzyme can also be an adaptor. The full mechanistic body was not recovered; the 2025 image correction is recorded separately. Supporting Evidence: PMID:35122041 We further demonstrate that Aldob potentiates p53-mediated inhibition of G6PD in an Aldob-G6PD-p53 complex. This scaffolding effect is independent of Aldob enzymatic activity. |
| GO:1905856 negative regulation of pentose-phosphate shunt | IMP PMID:35122041 Aldolase B suppresses hepatocellular carcinogenesis by inhib... | KEEP AS NON CORE | Summary: ALDOB directly participates in inhibition of the pentose-phosphate pathway. Reason: The source reports direct G6PD interaction/inhibition and enhancement of p53-mediated inhibition through a ternary scaffold, providing a molecular route beyond an indirect growth phenotype. Mouse liver knockout/rescue and human HCC observations define the study context. Retain this regulatory process as non-core without extending the measured mechanism to all ALDOB-expressing tissues. Supporting Evidence: PMID:35122041 Here we show that hepatic aldolase B (Aldob) suppresses HCC by directly binding and inhibiting the rate-limiting enzyme in the pentose phosphate pathway, glucose-6-phosphate dehydrogenase (G6PD). PMID:35122041 We further demonstrate that Aldob potentiates p53-mediated inhibition of G6PD in an Aldob-G6PD-p53 complex. This scaffolding effect is independent of Aldob enzymatic activity. |
| GO:0004332 fructose-bisphosphate aldolase activity | IDA PMID:10970798 Functional and molecular modelling studies of two hereditary... | ACCEPT | Summary: Human ALDOB kinetics establish bisphosphate aldolase catalysis. Reason: PMID:10970798 compares expressed wild-type human ALDOB with R303Q and R303W variants, measuring turnover of fructose 1,6-bisphosphate. Its structural interpretation uses homology models, not new crystal structures of those mutants. Supporting Evidence: PMID:10970798 The catalytic efficiency of protein Gln(303) is approx. 1/100 that of the wild-type for substrates fructose 1,6-bisphosphate and fructose 1-phosphate. |
| GO:0006096 glycolytic process | IDA PMID:10970798 Functional and molecular modelling studies of two hereditary... | ACCEPT | Summary: The measured ALDOB reaction directly performs a glycolytic step. Reason: The human enzyme measurements in PMID:10970798 establish F1,6BP cleavage. That chemically defined step belongs to glycolysis; the process inference does not require the paper to measure whole-cell glycolytic flux. Supporting Evidence: PMID:10970798 The catalytic efficiency of protein Gln(303) is approx. 1/100 that of the wild-type for substrates fructose 1,6-bisphosphate and fructose 1-phosphate. Reactome:R-HSA-71496 Cytosolic aldolase catalyzes the cleavage of D-fructose 1,6-bisphosphate to yield dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate. |
| GO:0061609 fructose-1-phosphate aldolase activity | IDA PMID:10970798 Functional and molecular modelling studies of two hereditary... | ACCEPT | Summary: The human enzyme has directly measured F1P activity. Reason: PMID:10970798 assays wild-type and two R303 variants with fructose 1-phosphate. The reduced or absent variant activities are interpreted relative to the active wild-type protein, supporting the specific F1P aldolase function. Supporting Evidence: PMID:10970798 The catalytic efficiency of protein Gln(303) is approx. 1/100 that of the wild-type for substrates fructose 1,6-bisphosphate and fructose 1-phosphate. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5656438 | ACCEPT | Summary: The disease event retains ALDOB in the cytosolic compartment. Reason: The live Reactome:R-HSA-5656438 record explicitly assigns cytosol to a defective-ALDOB event. That source concerns mutant loss of F1P cleavage and is not an independent wild-type positive catalytic assay. The compartment itself is consistent with independent human cytosolic ALDOB evidence and is retained. The recovered normal event summary now confirms the defective-enzyme context locally; the compartment was independently checked on the live human event. Supporting Evidence: Reactome:R-HSA-71496 Cytosolic aldolase catalyzes the cleavage of D-fructose 1,6-bisphosphate to yield dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate. |
| GO:0061609 fructose-1-phosphate aldolase activity | IDA PMID:2649152 Construction and expression of human aldolase A and B expres... | ACCEPT | Summary: Recombinant human ALDOB supports the F1P aldolase reaction. Reason: PMID:2649152 expresses human ALDOB in E. coli and reports enzymatic activity and the F1,6BP/F1P activity ratio. The authors note differences in net charge and the F1,6BP Km from an earlier liver preparation, so identity of every kinetic parameter is not asserted. Supporting Evidence: PMID:2649152 Enzymatically active forms of human aldolase have been generated in the cells when transfected with either pHAA47, a human aldolase A expression plasmid, or pHAB 141, a human aldolase B expression plasmid. PMID:10970798 The catalytic efficiency of protein Gln(303) is approx. 1/100 that of the wild-type for substrates fructose 1,6-bisphosphate and fructose 1-phosphate. |
| GO:0070062 extracellular exosome | HDA PMID:23533145 In-depth proteomic analyses of exosomes isolated from expres... | UNDECIDED | Summary: The source-specific ALDOB extracellular-vesicle identification remains unresolved. Reason: PMID:23533145 analyzes exosome-enriched expressed-prostatic-secretion urine pools. The full cached article establishes the preparation and proteomic screen, but the ALDOB-specific supplementary peptide entry was not recovered and no independent target-specific vesicle evidence was established here. Defer to the curator while leaving this HDA assertion UNDECIDED pending the target hit; this is an access limit, not evidence of contamination, a false identification or absence from exosomes. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-70342 | ACCEPT | Summary: The live F1P-cleavage event explicitly places ALDOB in cytosol. Reason: Reactome:R-HSA-70342 describes a cytosolic ALDOB tetramer cleaving fructose 1-phosphate to glyceraldehyde and DHAP. The live event and independent human biochemistry support this compartment. The recovered normal summary now supplies the same compartment and reaction wording locally. Supporting Evidence: Reactome:R-HSA-70342 Cytosolic aldolase B (ALDOB) catalyzes the reaction of D-fructose 1-phosphate (Fru 1-P) to form dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde (GA) PMID:10970798 The catalytic efficiency of protein Gln(303) is approx. 1/100 that of the wild-type for substrates fructose 1,6-bisphosphate and fructose 1-phosphate. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-71495 | ACCEPT | Summary: The reverse aldol-condensation event is cytosolic. Reason: The cached Reactome:R-HSA-71495 reaction explicitly locates formation of fructose 1,6-bisphosphate from the two triose phosphates in cytosol. ALDOB is one of the active aldolase isozymes; no unique location relative to ALDOA or ALDOC is implied. Supporting Evidence: Reactome:R-HSA-71495 In this freely reversible cytosolic reaction, DHAP (dihydroxyacetone phosphate) and GA3P (D-glyceraldehyde 3-phosphate) react to form F1,6PP (D-fructose 1,6-bisphosphate). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-71496 | ACCEPT | Summary: The canonical aldol-cleavage event is cytosolic. Reason: Cached Reactome:R-HSA-71496 explicitly places aldolase-mediated F1,6BP cleavage in cytosol. The statement about equivalent aldolase isozymes pertains to this reaction and should not be generalized to equal F1P substrate kinetics. Supporting Evidence: Reactome:R-HSA-71496 Cytosolic aldolase catalyzes the cleavage of D-fructose 1,6-bisphosphate to yield dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate. |
| GO:0004332 fructose-bisphosphate aldolase activity | IDA PMID:17576770 Physical interaction between aldolase and vacuolar H+-ATPase... | ACCEPT | Summary: The V-ATPase study includes ALDOB catalytic controls. Reason: The full PMID:17576770 study measures human ALDOB and binding-defective A318E catalytic activity while separating it from V-ATPase association. These positive activity controls support the aldolase MF; the coupled assay does not make ALDOB itself an NADH oxidoreductase. Supporting Evidence: PMID:17576770 In this study, we generate aldolase mutants that lack binding to the B subunit of V-ATPase but retain normal catalytic activities. PMID:10625657 We describe the biochemical and biophysical characterization of seven natural human aldolase B variants, identified in patients suffering from hereditary fructose intolerance and expressed as recombinant proteins in E. coli, from which they were purified to homogeneity. |
| GO:0004332 fructose-bisphosphate aldolase activity | IDA PMID:9244396 Mode of interactions of human aldolase isozymes with cytoske... | ACCEPT | Summary: Retain the curated catalytic activity from the isozyme comparison. Reason: PMID:9244396 compares human aldolase isozymes and their cytoskeletal interactions. The cached abstract gives a positive ALDOB result but foregrounds ALDOA for detailed substrate-competition and mutant experiments. Retain the curated ALDOB activity in light of independent human kinetics, without attributing every ALDOA assay to ALDOB. Supporting Evidence: PMID:10970798 The catalytic efficiency of protein Gln(303) is approx. 1/100 that of the wild-type for substrates fructose 1,6-bisphosphate and fructose 1-phosphate. |
| GO:0006000 fructose metabolic process | IMP PMID:3383242 Catalytic deficiency of human aldolase B in hereditary fruct... | ACCEPT | Summary: Human ALDOB deficiency and enzyme chemistry support fructose metabolism. Reason: PMID:3383242 identifies an HFI-associated ALDOB lesion in patients, explicitly describing the resulting inability to metabolize fructose. This is a genotype/deficient-protein study, not a new purified-enzyme kinetic experiment. Independent ALDOB F1P cleavage establishes direct pathway participation. Supporting Evidence: PMID:3383242 Hereditary fructose intolerance (HFI) is a human autosomal recessive disease caused by a deficiency of aldolase B that results in an inability to metabolize fructose and related sugars. PMID:10970798 The catalytic efficiency of protein Gln(303) is approx. 1/100 that of the wild-type for substrates fructose 1,6-bisphosphate and fructose 1-phosphate. |
| GO:0008092 cytoskeletal protein binding | IDA PMID:9244396 Mode of interactions of human aldolase isozymes with cytoske... | KEEP AS NON CORE | Summary: Retain the direct human ALDOB cytoskeletal-binding observation. Reason: PMID:9244396 explicitly reports that liver-type aldolase B prefers liver cytoskeleton. This supports the broad cytoskeletal protein-binding term as a non-core interaction. The detailed ALDOA mutant, fibroblast and contraction experiments cannot be silently transferred to ALDOB or used to assert an ALDOB contraction mechanism. Supporting Evidence: PMID:9244396 Aldolase A (muscle type) bound more tightly to the skeletal muscle cytoskeleton among the three isozymes, while aldolase B (liver type) preferred the liver cytoskeleton to those of other tissues. |
| GO:0030388 fructose 1,6-bisphosphate metabolic process | IDA PMID:9244396 Mode of interactions of human aldolase isozymes with cytoske... | ACCEPT | Summary: The substrate-process annotation is consistent with ALDOB catalytic chemistry. Reason: The isozyme comparison PMID:9244396 includes human ALDOB, and direct independent kinetics establish its F1,6BP reaction. Retain the process annotation while recognizing that the accessible source abstract places most detailed substrate-competition assays on ALDOA. Supporting Evidence: PMID:10970798 The catalytic efficiency of protein Gln(303) is approx. 1/100 that of the wild-type for substrates fructose 1,6-bisphosphate and fructose 1-phosphate. |
| GO:0051117 ATPase binding | IDA PMID:17576770 Physical interaction between aldolase and vacuolar H+-ATPase... | KEEP AS NON CORE | Summary: Human ALDOB binding to V-ATPase has a measured assembly consequence. Reason: Full PMID:17576770 experiments distinguish human ALDOB binding to the V-ATPase B subunit from aldolase catalysis, including human constructs expressed in yeast. ATPase binding is an informative, experimentally grounded non-core MF here; it does not imply that ALDOB hydrolyzes ATP or transports protons. Supporting Evidence: PMID:17576770 Functional analysis of the aldolase mutants shows that disruption of binding between aldolase and the B subunit of V-ATPase results in disassembly and malfunction of V-ATPase. |
| GO:0070061 fructose binding | IMP PMID:10625657 Expression, purification, and characterization of natural mu... | REMOVE | Summary: The complete cited assays concern fructose phosphates, not free fructose. Reason: GO:0070061 explicitly denotes binding to unphosphorylated fructose. PMID:10625657 Methods/Results measure F1P and F1,6BP cleavage, phosphorylated-substrate affinity elution and DHAP/glyceraldehyde condensation. Its mutant binding interpretation concerns phosphate-bearing substrates. Remove the unsupported free-fructose assignment rather than change binding into a catalytic category; the aldolase activities already capture the supported chemistry. This source mismatch does not prove that ALDOB could never bind free fructose. Supporting Evidence: PMID:10625657 We describe the biochemical and biophysical characterization of seven natural human aldolase B variants, identified in patients suffering from hereditary fructose intolerance and expressed as recombinant proteins in E. coli, from which they were purified to homogeneity. PMID:10970798 The catalytic efficiency of protein Gln(303) is approx. 1/100 that of the wild-type for substrates fructose 1,6-bisphosphate and fructose 1-phosphate. |
| GO:0004332 fructose-bisphosphate aldolase activity | IDA PMID:10625657 Expression, purification, and characterization of natural mu... | ACCEPT | Summary: Purified recombinant human ALDOB directly cleaves F1,6BP. Reason: PMID:10625657 measures cleavage kinetics with purified wild-type and natural human ALDOB variants. The controlled substrate assays directly support this molecular function, with mutant oligomerization explaining part of the activity loss. Supporting Evidence: PMID:10625657 We describe the biochemical and biophysical characterization of seven natural human aldolase B variants, identified in patients suffering from hereditary fructose intolerance and expressed as recombinant proteins in E. coli, from which they were purified to homogeneity. PMID:10625657 Investigation of these two classes of mutant enzyme suggests that the integrity of the quaternary structure of aldolase B is critical for maintaining its full catalytic function. |
| GO:0006096 glycolytic process | IDA PMID:10625657 Expression, purification, and characterization of natural mu... | ACCEPT | Summary: ALDOB directly executes the glycolytic aldolase reaction. Reason: PMID:10625657 establishes purified human F1,6BP cleavage. This is a catalytic step of glycolysis, not simply a correlation between ALDOB abundance and glycolytic gene expression. The enzyme is not itself the NADH-oxidizing component of the coupled assay. Supporting Evidence: PMID:10625657 Fructaldolases (EC 4.1.2.13) are ancient enzymes of glycolysis that catalyze the reversible cleavage of phosphofructose esters into cognate triose (phosphates). PMID:10625657 We describe the biochemical and biophysical characterization of seven natural human aldolase B variants, identified in patients suffering from hereditary fructose intolerance and expressed as recombinant proteins in E. coli, from which they were purified to homogeneity. |
| GO:0030388 fructose 1,6-bisphosphate metabolic process | IDA PMID:10625657 Expression, purification, and characterization of natural mu... | ACCEPT | Summary: Measured F1,6BP turnover supports the substrate-metabolism process. Reason: The complete PMID:10625657 substrate assays directly demonstrate ALDOB action on fructose 1,6-bisphosphate. This accurate process-level assertion is retained alongside the specific MF; no additional redundant process annotation is proposed. Supporting Evidence: PMID:10625657 Fructaldolases (EC 4.1.2.13) are ancient enzymes of glycolysis that catalyze the reversible cleavage of phosphofructose esters into cognate triose (phosphates). PMID:10625657 We describe the biochemical and biophysical characterization of seven natural human aldolase B variants, identified in patients suffering from hereditary fructose intolerance and expressed as recombinant proteins in E. coli, from which they were purified to homogeneity. |
| GO:0042802 identical protein binding | IPI PMID:10625657 Expression, purification, and characterization of natural mu... | ACCEPT | Summary: Homotetrameric assembly is a functional component of ALDOB catalysis. Reason: PMID:10625657 studies purified human ALDOB and shows that several natural variants destabilize homotetramers with impaired activity. The self-partner P05062 and quaternary-structure measurements support identical-protein binding as core assembly evidence. This is distinct from the ALDOA heterologous interaction records. Supporting Evidence: PMID:10625657 Investigation of these two classes of mutant enzyme suggests that the integrity of the quaternary structure of aldolase B is critical for maintaining its full catalytic function. |
| GO:0034451 centriolar satellite | IDA PMID:18000879 Novel interaction partners of Bardet-Biedl syndrome proteins... | KEEP AS NON CORE | Summary: Retain the experimentally inferred peripheral centrosomal distribution. Reason: The full PMID:18000879 paper shows transfected EGFP-ALDOB adjacent to gamma-tubulin in HeLa cells and discusses possible partial localization at centriolar satellites. Retain this curator-interpreted IDA compartment as non-core with the observed uncertainty; the study does not establish native hepatocyte satellite function. Supporting Evidence: |
| GO:0005815 microtubule organizing center | IDA PMID:18000879 Novel interaction partners of Bardet-Biedl syndrome proteins... | KEEP AS NON CORE | Summary: Retain the observed MTOC-associated pool as non-core. Reason: The full BBS study reports ALDOB/BBS colocalizing puncta near the centrosome, described as presumably the microtubule organizing center. The location is experimentally motivated but imprecise and based on transfected HeLa cells. Retain the broad compartment without asserting microtubule nucleation or a direct role in centrosome assembly. Supporting Evidence: |
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Download this section (compressed HTML)Q: Should GO:0070061 be removed from ALDOB when the cited experiments concern fructose 1-phosphate and fructose 1,6-bisphosphate rather than unphosphorylated fructose? A phosphate-sugar interaction term, if needed, must preserve ligand specificity rather than duplicate the catalytic annotations.
Q: How do the historical PAINT PTN000179343 annotations correspond to the current PTHR11627 IBD at PTN004279385?
Q: What original ALDOB experiments support the source-specific EXP assignments to PMID:6696436 and the metadata-only PMID:12205126 record?
Q: How broadly do endogenous human ALDOB-G6PD-p53 scaffolding and ALDOB-dependent V-ATPase assembly operate outside the hepatic tumor models and heterologous yeast assays, respectively?
Q: Does endogenous ALDOB localize to defined centriolar satellites in physiologically expressing human cells, beyond the transfected-HeLa peripheral centrosomal pattern?
Q: Should ALDOA and PFKM fructose-binding judgments be revisited where they equate phosphorylated substrates with free fructose? Their existing ACCEPT reasons invoke F1,6BP or F6P, but GO:0070061 is on the monosaccharide-binding branch and GO:0070095 is on the carbohydrate-derivative-binding branch. The shared ARBA00092505 mapping also warrants source-level review. This is a scoped follow-up question, not an automatic reversal of those genes without their primary evidence.
Experiment: Compare purified human ALDOB binding to free fructose, F1P and F1,6BP with catalysis-independent affinity measurements, using catalytic and oligomerization controls.
Experiment: Measure endogenous ALDOB-dependent G6PD-p53 complex formation and pentose-phosphate flux across primary human liver, kidney and intestinal cells, separating catalytic rescue from interaction-selective rescue.
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