Aldolase C
| ALDOC | |||
|---|---|---|---|
Gene ontology | |||
| Molecular function | |||
| Cellular component | |||
| Biological process | |||
| Sources:Amigo / QuickGO | |||
Ensembl | |||||||||
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| UniProt | |||||||||
| RefSeq (mRNA) | |||||||||
| RefSeq (protein) | |||||||||
| Location (UCSC) | Chr 17: 28.57 – 28.58 Mb | Chr 11: 78.21 – 78.22 Mb | |||||||
| PubMed search | [3] | [4] | |||||||
| View/Edit Human | View/Edit Mouse |
Aldolase C, fructose-bisphosphate (ALDOC, or ALDC), is an
fructose-1-phosphate to dihydroxyacetone phosphate and either glyceraldehyde 3-phosphate or glyceraldehyde, respectively.[provided by RefSeq, Jul 2008][5][6]
Structure
ALDOC is one of the three aldolase
electrostatic surface of ALDOC is more negatively charged, which may serve as an acidic binding site or as a docking site to accommodate the C-terminal conformations.[8] Four ALDOC-specific residues (N90, V92, R96 and D100) may be key for ALDOC-specific functions.[9]
Function
ALDOC is a key enzyme in the fourth step of glycolysis, as well as in the reverse pathway
cerebellar Purkinje cells against excitotoxic insult.[10]
ALDOC is ubiquitously expressed in most tissues, though it is predominantly expressed in
ALDOA isoform is co-expressed with ALDOC in the central nervous system (CS), it is suggested that ALDOC contributes to CNS function outside of glycolysis.[9] Moreover, its presence within other cell types, such as platelets and mast cells (MCs), may serve as a failsafe in the case that the other predominant aldolase isozymes become inactivated.[11] Within cells, it localizes to the cytoplasm.[12]
Clinical significance
This aldolase has been associated with cancer.[8]
ALDOC is found to be upregulated in the brains of schizophrenia (SCZ) patients.[13] Notably, while ALDOC is differentially expressed in the anterior cingulate cortex (ACC) of male SCZ patients, it displays no significant changes in female SCZ patients, indicating that different regulatory mechanisms may be involved in male versus female SCZ patients. It is likely that ALDOC is involved in SCZ through its role in glycolysis, which is a central biochemical pathway in SCZ.[14]
Furthermore, ALDOC is reported to undergo
oxidation in brains affected by mild cognitive impairment (MCI) and Alzheimer's disease (AD). This oxidative modification inhibits ALDOC activity, causing the accumulation of fructose 1,6- bisphosphate and driving the reverse reaction, in the direction of gluconeogenesis rather than glycolysis, thus halting ATP production.[15]
Interactive pathway map
Click on genes, proteins and metabolites below to link to respective articles.[§ 1]
Glycolysis and Gluconeogenesis edit
- ^ The interactive pathway map can be edited at WikiPathways: "GlycolysisGluconeogenesis_WP534".
See also
- ALDOA
- ALDOB
- Fructose-bisphosphate aldolase
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000109107 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000017390 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Entrez Gene: ALDOC aldolase C, fructose-bisphosphate".
- S2CID 7980799.
- PMID 24465716.
- ^ PMID 15537755.
- ^ PMID 24525694.
- S2CID 46706309.
- ^ PMID 20511553.
- ^ PMID 23886627.
- PMID 19110265.
- PMID 20381070.
- PMID 19686046.
Further reading
- Buono P, Mancini FP, Izzo P, Salvatore F (September 1990). "Characterization of the transcription-initiation site and of the promoter region within the 5' flanking region of the human aldolase C gene". European Journal of Biochemistry. 192 (3): 805–11. PMID 2209624.
- Rocchi M, Vitale E, Covone A, Romeo G, Santamaria R, Buono P, Paolella G, Salvatore F (June 1989). "Assignment of human aldolase C gene to chromosome 17, region cen----q21.1". Human Genetics. 82 (3): 279–82. S2CID 7980799.
- Rottmann WH, Deselms KR, Niclas J, Camerato T, Holman PS, Green CJ, Tolan DR (February 1987). "The complete amino acid sequence of the human aldolase C isozyme derived from genomic clones". Biochimie. 69 (2): 137–45. PMID 3105602.
- Buono P, Paolella G, Mancini FP, Izzo P, Salvatore F (May 1988). "The complete nucleotide sequence of the gene coding for the human aldolase C". Nucleic Acids Research. 16 (10): 4733. PMID 3267224.
- Tolan DR, Niclas J, Bruce BD, Lebo RV (November 1987). "Evolutionary implications of the human aldolase-A, -B, -C, and -pseudogene chromosome locations". American Journal of Human Genetics. 41 (5): 907–24. PMID 3674018.
- Penhoet E, Rajkumar T, Rutter WJ (October 1966). "Multiple forms of fructose diphosphate aldolase in mammalian tissues". Proceedings of the National Academy of Sciences of the United States of America. 56 (4): 1275–82. PMID 5230152.
- Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (April 1996). "A "double adaptor" method for improved shotgun library construction". Analytical Biochemistry. 236 (1): 107–13. PMID 8619474.
- Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA (April 1997). "Large-scale concatenation cDNA sequencing". Genome Research. 7 (4): 353–8. PMID 9110174.
- Kim JH, Lee S, Kim JH, Lee TG, Hirata M, Suh PG, Ryu SH (March 2002). "Phospholipase D2 directly interacts with aldolase via Its PH domain". Biochemistry. 41 (10): 3414–21. PMID 11876650.
- Arakaki TL, Pezza JA, Cronin MA, Hopkins CE, Zimmer DB, Tolan DR, Allen KN (December 2004). "Structure of human brain fructose 1,6-(bis)phosphate aldolase: linking isozyme structure with function". Protein Science. 13 (12): 3077–84. PMID 15537755.
- Buono P, Barbieri O, Alfieri A, Rosica A, Astigiano S, Cantatore D, Mancini A, Fattoruso O, Salvatore F (December 2004). "Diverse human aldolase C gene promoter regions are required to direct specific LacZ expression in the hippocampus and Purkinje cells of transgenic mice". FEBS Letters. 578 (3): 337–44. S2CID 41355547.
- Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y (August 2006). "Substrate and functional diversity of lysine acetylation revealed by a proteomics survey". Molecular Cell. 23 (4): 607–18. PMID 16916647.
External links
- Human ALDOC genome location and ALDOC gene details page in the UCSC Genome Browser.
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