| Topic | Key finding | Quantitative details (fold change, FDR/p-adj, lifespan %) | System/condition (strain/tissue) | Source (authors, year, journal) | Publication date (month/year) | URL/DOI | Evidence strength/notes |
|---|---|---|---|---|---|---|---|
| Identity | UniProt P54216 is listed as **Caenorhabditis elegans FBA 1**, supporting assignment of the target protein to C. elegans fructose-bisphosphate aldolase 1. | None reported in snippet. | Comparative aldolase phylogeny; C. elegans sequence entry. | Pirovich et al., 2021, *Frontiers in Molecular Biosciences* | Aug 2021 | https://doi.org/10.3389/fmolb.2021.719678 | Useful accession-level confirmation for P54216; review/phylogeny rather than direct worm functional experiment. (pqac-00000010) |
| Identity | ORF **T05D4.1** is explicitly annotated as **aldo-1**, “fructose bisphosphate aldolase,” confirming aldo-1 ↔ T05D4.1 mapping in C. elegans. | Male:hermaphrodite ratios shown for two transcript entries: T05D4.1.2 = **2.11*** (young adult), **2.85*** (adult); T05D4.1.1 = **2.12*** (young adult), **2.33** (adult). | Whole-animal sex-comparison transcriptomics in young adult and adult worms. | Miersch & Döring, 2012, *PLoS ONE* | Sep 2012 | https://doi.org/10.1371/journal.pone.0044748 | Strong direct mapping for the gene name/ORF in C. elegans; asterisks indicate significance but exact p-value thresholds were not present in snippet. (pqac-00000012, pqac-00000004) |
| Function | aldo-1 is a glycolytic **fructose-bisphosphate aldolase** catalyzing cleavage of **fructose-1,6-bisphosphate** toward **glyceraldehyde-3-phosphate** (table wording shows reaction direction). | Reaction shown as “fructose-1,6 bisphosphate → glyceraldehyd-3 phosphate” in the table; aldolase is also described as catalyzing the fourth step of glycolysis. | C. elegans carbohydrate metabolism annotation; general aldolase biochemistry review. | Miersch & Döring, 2012, *PLoS ONE*; Pirovich et al., 2021, *Frontiers in Molecular Biosciences* | Sep 2012; Aug 2021 | https://doi.org/10.1371/journal.pone.0044748 ; https://doi.org/10.3389/fmolb.2021.719678 | Strong for pathway-level enzymatic role; the full stoichiometric coproduct list is not fully printed in the Miersch table snippet, but aldolase substrate context is explicit. (pqac-00000012, pqac-00000010) |
| Function / mechanism | Aldolases of this family use a **class I Schiff-base mechanism**; conserved active-site residues are retained in nematode homologs including C. elegans aldo-1 in sequence alignment context. | In homologous enzyme model, **Lys230** is the Schiff-base residue; kinetic values for recombinant nematode aldolase: **Km = 0.24 ± 0.01 µM**, **Vmax = 432 nmol min−1 mg−1**, optimum **pH 7.5**, **n = 3**. | Comparative nematode aldolase biochemistry/structure (Teladorsagia with C. elegans aldo-1 in alignment). | Umair et al., 2021, *Parasitologia* | Jan 2021 | https://doi.org/10.3390/parasitologia1010001 | Indirect but informative for ALDO-1 because the study includes C. elegans aldo-1 among homologs and highlights conserved catalytic residues typical of class I aldolases. (pqac-00000011, pqac-00000001) |
| Expression-regulation | aldo-1 expression is higher in **males** than in **hermaphrodites**, consistent with sex-biased carbohydrate metabolism. | Male:hermaphrodite expression ratios: **2.11*** and **2.12*** in young adults; **2.85*** and **2.33** in adults for two T05D4.1 transcript entries. | Whole animals; young adult and adult stages. | Miersch & Döring, 2012, *PLoS ONE* | Sep 2012 | https://doi.org/10.1371/journal.pone.0044748 | Direct C. elegans evidence; no tissue localization given in snippet. (pqac-00000012, pqac-00000004) |
| Pathway / phenotype | In mitochondrial complex I mutants, aldo-1 is strongly upregulated, supporting increased glycolytic dependence. | **~3-fold** increase in **gas-1(fc21)**; **~6-fold** increase in **nuo-6(qm200)**. | Day-1 adults from synchronized populations; qRT-PCR in mitochondrial mutant worms. | Pujol et al., 2013, *PLoS ONE* | Mar 2013 | https://doi.org/10.1371/journal.pone.0059493 | Strong direct evidence connecting aldo-1 to metabolic rewiring in vivo. (pqac-00000009, pqac-00000002) |
| Phenotype | aldo-1 is functionally important for survival/longevity of complex I mutants; RNAi knockdown greatly shortens lifespan. | In **gas-1(fc21)**, median lifespan decreased by **up to 65%** after aldo-1 RNAi; in **nuo-6(qm200)**, aldo-1 downregulation decreased median lifespan by **>85%**. | RNAi in mitochondrial complex I mutant worms. | Pujol et al., 2013, *PLoS ONE* | Mar 2013 | https://doi.org/10.1371/journal.pone.0059493 | Strong phenotype-to-function link; indicates reliance on glycolysis when respiration is impaired. (pqac-00000009, pqac-00000002) |
| Pathway | Authors conclude both complex I mutants “**rely heavily on glycolysis for energy production**,” placing aldo-1 in compensatory metabolic adaptation. | Lifespan sensitivity to aldo-1 RNAi as above; icl-1 had milder effects by comparison. | gas-1(fc21) and nuo-6(qm200) mitochondrial dysfunction models. | Pujol et al., 2013, *PLoS ONE* | Mar 2013 | https://doi.org/10.1371/journal.pone.0059493 | Strong pathway inference because supported by expression plus functional RNAi data. (pqac-00000009, pqac-00000002) |
| Recent studies | Persistent **HIF-1 over-activation** upregulates aldo-1 as part of a shared metabolic response in three HIF-1 high-activity mutants. | aldo-1 is in the **104 genes** upregulated in all three mutants; enriched WormCat **Cat1: Metabolism**, **23 genes**, **Bonferroni FDR = 9.23E-07**; overlaps significant at **p < 2.2E-16**. | C. elegans **vhl-1(ok161)**, **egl-9(sa307)**, **rhy-1(ok1402)** mutants. | Feng et al., 2024, *PLOS ONE* | Mar 2024 | https://doi.org/10.1371/journal.pone.0295093 | Strong recent evidence for transcriptional regulation in hypoxia/HIF biology; no gene-specific fold change for aldo-1 in snippet. (pqac-00000014, pqac-00000003) |
| Recent studies / tissue context | In **aging male neurons**, aldo-1 is among glycolytic genes that decline with age, linking it to neuronal energetic aging. | Downregulated with age by **at least 2-fold**; significance framework in study used **DESeq2**, cutoff **log2 fold-change > 0.5 or < -0.5, p-adj < 0.05**. | Sorted **male neurons** during aging; compared young vs aged neuronal transcriptomes. | Weng & Murphy, 2024, *iScience* | Jun 2024 | https://doi.org/10.1016/j.isci.2024.109910 | Strong recent tissue-specific transcriptomic evidence; snippet does not provide aldo-1-specific adjusted p-value. (pqac-00000013, pqac-00000006, pqac-00000008) |
| Expression/localization | Direct subcellular localization of C. elegans ALDO-1 was **not provided** in the retrieved worm-specific snippets; canonical aldolase literature describes aldolase as a **cytosolic** glycolytic enzyme, with moonlighting/extracellular roles in other systems. | None for C. elegans ALDO-1 in snippets. | General aldolase biology review; not worm-specific localization experiment. | Pirovich et al., 2021, *Frontiers in Molecular Biosciences* | Aug 2021 | https://doi.org/10.3389/fmolb.2021.719678 | Caution: relevant for family-level inference, not direct localization evidence for C. elegans aldo-1. (pqac-00000010) |
| Applications | Aldolase is highlighted broadly as a **therapeutic target**, with inhibitor and vaccine interest in pathogens; this supports translational relevance of conserved aldolase biology, though not a direct C. elegans application. | No C. elegans-specific implementation metrics in snippet. | Cross-species/pathogen aldolase biology. | Pirovich et al., 2021, *Frontiers in Molecular Biosciences* | Aug 2021 | https://doi.org/10.3389/fmolb.2021.719678 | Indirect application relevance only; useful for contextualizing why conserved aldolases are studied. (pqac-00000010) |


*Table: This table summarizes the available evidence for the functional annotation of C. elegans aldo-1/P54216/T05D4.1, including identity mapping, enzymatic role, pathway context, regulatory patterns, phenotypes, and recent 2024 studies. It is useful as a citation-linked overview of what is directly supported by the retrieved snippets versus what remains inferred.*