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Aldolase A, fructose-bisphosphate
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| PDB rendering based on 4ALD. The Protein Data Bank ( PDB) is a repository for 3-D structural data of Proteins and Nucleic acids These data typically obtained by X-ray crystallography |
| Available structures: 1ado, 1ald, 1ewd, 1ewe, 1ewg, 1ex5, 1j4e, 1zah, 1zai, 1zaj, 1zal, 2ald, 2ot0, 2ot1, 4ald, 6ald |
| Identifiers |
| Symbol(s) |
ALDOA; ALDA; MGC10942; MGC17716; MGC17767 |
| External IDs |
OMIM: 103850 MGI: 87994 HomoloGene: 68996 |
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| RNA expression pattern |
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More reference expression data
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| Orthologs |
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Human |
Mouse |
| Entrez |
226 |
11674 |
| Ensembl |
ENSG00000149925 |
ENSMUSG00000030695 |
| Uniprot |
P04075 |
Q5FWB7 |
| Refseq |
NM_000034 (mRNA)
NP_000025 (protein) |
NM_007438 (mRNA)
NP_031464 (protein) |
| Location |
Chr 16: 29.97 - 29.99 Mb |
Chr 7: 126.59 - 126.59 Mb |
| Pubmed search |
[1] |
[2] |
Aldolase A is an enzyme which catalyses one of the aldol reactions: The substrate, fructose 1,6-bisphosphate (F-1,6-BP) is broken down into glyceraldehyde 3-phosphate and dihydroxyacetone phosphate (DHAP). The Human Genome Organisation (HUGO is an organization involved in the Human Genome Project, a project about mapping the human genome The Mouse Genome Informatics (MGI website is run by The Jackson Laboratory. HomoloGene, a tool of the National Center for Biotechnology Information (NCBI is a system for automated detection of homologs (similarity attributable to descent The Entrez Global Query Cross-Database Search System is a powerful Federated search engine or Web portal that allows users to search many discrete Health sciences Ensembl is a joint scientific project between the European Bioinformatics Institute and the Wellcome Trust Sanger Institute, which was launched in 1999 in response to the imminent UniProt is the uni versal prot ein resource a central repository of Protein data created by combining Swiss-Prot, TrEMBL PubMed is a free search engine for accessing the MEDLINE database of citations and abstracts of biomedical research articles Enzymes are Biomolecules that catalyze ( ie increase the rates of Chemical reactions Almost all enzymes are Proteins The aldol reaction is an important Carbon-carbon bond formation reaction in Organic chemistry. Fructose 16-phosphate is Fructose sugar Phosphorylated on carbons 1 and 6 (ie Glyceraldehyde 3-phosphate, also known as triose phosphate or 3-phosphoglyceraldehyde and abbreviated as G3P, GADP, GAP or PGAL Dihydroxyacetone phosphate (DHAP is a biochemical compound involved in many reactions from the Calvin cycle in plants to the ether-lipid biosynthesis process in Leishmania Dihydroxyacetone phosphate (DHAP is a biochemical compound involved in many reactions from the Calvin cycle in plants to the ether-lipid biosynthesis process in Leishmania This reaction is a part of glycolysis. See also Gluconeogenesis, which carries out a process wherein glucose is synthesized rather than catabolized Three aldolase isozymes (A, B, and C), encoded by three different genes, are differentially expressed during development. Aldolase A is found in the developing embryo and is produced in even greater amounts in adult muscle. Aldolase A expression is repressed in adult liver, kidney and intestine and similar to aldolase C levels in brain and other nervous tissue. Aldolase A deficiency has been associated with myopathy and hemolytic anemia. Alternative splicing of this gene results in multiple transcript variants which encode the same protein. [1]
Compound C05378 at KEGG Pathway Database. Fructose 16-phosphate is Fructose sugar Phosphorylated on carbons 1 and 6 (ie Aldolase A is an Enzyme which catalyses one of the Aldol reactions: The substrate, Fructose 16-bisphosphate (F-16-BP is broken down into Glyceraldehyde 3-phosphate, also known as triose phosphate or 3-phosphoglyceraldehyde and abbreviated as G3P, GADP, GAP or PGAL Dihydroxyacetone phosphate (DHAP is a biochemical compound involved in many reactions from the Calvin cycle in plants to the ether-lipid biosynthesis process in Leishmania Aldolase A is an Enzyme which catalyses one of the Aldol reactions: The substrate, Fructose 16-bisphosphate (F-16-BP is broken down into KEGG ( Kyoto Encyclopedia of Genes and Genomes) is a collection of Online databases dealing with Genomes Enzymatic pathways and biological chemicals Enzyme 4.1.2.13 at KEGG Pathway Database. KEGG ( Kyoto Encyclopedia of Genes and Genomes) is a collection of Online databases dealing with Genomes Enzymatic pathways and biological chemicals Compound C00111 at KEGG Pathway Database. KEGG ( Kyoto Encyclopedia of Genes and Genomes) is a collection of Online databases dealing with Genomes Enzymatic pathways and biological chemicals Compound C00118 at KEGG Pathway Database. KEGG ( Kyoto Encyclopedia of Genes and Genomes) is a collection of Online databases dealing with Genomes Enzymatic pathways and biological chemicals
The numbering of the carbon atoms indicates the fate of the carbons according to their position in fructose 6-phosphate.
Mechanism
In mammalian aldolase the key catylitic amino acid residues involved in the reaction are lysine and tyrosine. In Chemistry, an amino acid is a Molecule containing both Amine and Carboxyl Functional groups In Biochemistry, this Lysine (abbreviated as Lys or K) is an α- Amino acid with the Chemical formula HO2CCH(NH2(CH24NH2 Tyrosine (abbreviated as Tyr or Y) or 4-hydroxyphenylalanine, is one of the 20 Amino acids that are used by cells to synthesize The tyrosine acts as an efficient hydrogen acceptor while the lysine covalently binds and stabilizes the intermediates. Many bacteria use two magnesium ions in place of the lysine. The Bacteria ( singular: bacterium) are a large group of unicellular Microorganisms Typically a few Micrometres in length bacteria have Magnesium (mægˈniːziəm is a Chemical element with the symbol Mg, Atomic number 12 Atomic weight 24 An ion is an Atom or Molecule which has lost or gained one or more Valence electrons giving it a positive or negative electrical charge
The reaction mechanism of aldolase.
The enzyme's reactive site amino acid's side chains are shown in blue.
Abbreviations: DHAP - dihydroxyacetone phosphate; Fru1,6bP - Fructose-1,6-bisphosphate; GAD - glyceraldehyde 3-phosphate;
References
Further reading
- Pfleiderer G, Thöner M, Wachsmuth ED (1976). "Histological examination of the aldolase monomer composition of cells from human kidney and hypernephroid carcinoma. ". Beiträge zur Pathologie 156 (3): 266-79. PMID 766744.
- Rehbein-Thöner M, Pfleiderer G (1977). "The changes in aldolase isoenzyme pattern during development of the human kidney and small intestine--demonstrated in organ extracts and tissue sections. ". Hoppe-Seyler's Z. Physiol. Chem. 358 (2): 169-80. PMID 844801.
- Wachsmuth ED (1976). "Differentiation of epithelial cells in human jejunum: localization and quantification of aminopeptidase, alkaline phosphatase and aldolase isozymes in tissue sections. ". Histochemistry 48 (2): 101-9. doi:10.1007/BF00494548. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document. PMID 955981.
- Lee KN, Maxwell MD, Patterson MK, et al. (1992). "Identification of transglutaminase substrates in HT29 colon cancer cells: use of 5-(biotinamido)pentylamine as a transglutaminase-specific probe. ". Biochim. Biophys. Acta 1136 (1): 12-6. doi:10.1016/0167-4889(92)90078-P. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document. PMID 1353685.
- Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. ". J. Infect. 24 (3): 317-20. doi:10.1016/S0163-4453(05)80037-4. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document. PMID 1602151.
- Mukai T, Arai Y, Yatsuki H, et al. (1991). "An additional promoter functions in the human aldolase A gene, but not in rat. ". Eur. J. Biochem. 195 (3): 781-7. doi:10.1111/j.1432-1033.1991.tb15766.x. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document. PMID 1999195.
- Gamblin SJ, Davies GJ, Grimes JM, et al. (1991). "Activity and specificity of human aldolases. ". J. Mol. Biol. 219 (4): 573-6. doi:10.1016/0022-2836(91)90650-U. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document. PMID 2056525.
- Vértessy BG, Orosz F, Ovádi J (1991). "Modulation of the interaction between aldolase and glycerol-phosphate dehydrogenase by fructose phosphates. ". Biochim. Biophys. Acta 1078 (2): 236-42. PMID 2065091.
- Takasaki Y, Takahashi I, Mukai T, Hori K (1990). "Human aldolase A of a hemolytic anemia patient with Asp-128----Gly substitution: characteristics of an enzyme generated in E. coli transfected with the expression plasmid pHAAD128G. ". J. Biochem. 108 (2): 153-7. PMID 2229018.
- Gamblin SJ, Cooper B, Millar JR, et al. (1990). "The crystal structure of human muscle aldolase at 3. 0 A resolution. ". FEBS Lett. 262 (2): 282-6. doi:10.1016/0014-5793(90)80211-Z. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document. PMID 2335208.
- Kishi H, Mukai T, Hirono A, et al. (1988). "Human aldolase A deficiency associated with a hemolytic anemia: thermolabile aldolase due to a single base mutation. ". Proc. Natl. Acad. Sci. U. S. A. 84 (23): 8623-7. doi:10.1073/pnas.84.23.8623. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document. PMID 2825199.
- Izzo P, Costanzo P, Lupo A, et al. (1987). "A new human species of aldolase A mRNA from fibroblasts. ". Eur. J. Biochem. 164 (1): 9-13. doi:10.1111/j.1432-1033.1987.tb10984.x. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document. PMID 3030757.
- Inagaki H, Haimoto H, Hosoda S, Kato K (1988). "Aldolase C is localized in neuroendocrine cells. ". Experientia 44 (9): 749-51. doi:10.1007/BF01959149. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document. PMID 3046960.
- Freemont PS, Dunbar B, Fothergill-Gilmore LA (1988). "The complete amino acid sequence of human skeletal-muscle fructose-bisphosphate aldolase. ". Biochem. J. 249 (3): 779-88. PMID 3355497.
- Izzo P, Costanzo P, Lupo A, et al. (1988). "Human aldolase A gene. Structural organization and tissue-specific expression by multiple promoters and alternate mRNA processing. ". Eur. J. Biochem. 174 (4): 569-78. doi:10.1111/j.1432-1033.1988.tb14136.x. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document. PMID 3391172.
- Maire P, Gautron S, Hakim V, et al. (1988). "Characterization of three optional promoters in the 5' region of the human aldolase A gene. ". J. Mol. Biol. 197 (3): 425-38. doi:10.1016/0022-2836(87)90556-0. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document. PMID 3441006.
- Kukita A, Yoshida MC, Fukushige S, et al. (1987). "Molecular gene mapping of human aldolase A (ALDOA) gene to chromosome 16. ". Hum. Genet. 76 (1): 20-6. doi:10.1007/BF00283044. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document. PMID 3570299.
- Tolan DR, Niclas J, Bruce BD, Lebo RV (1987). "Evolutionary implications of the human aldolase-A, -B, -C, and -pseudogene chromosome locations. ". Am. J. Hum. Genet. 41 (5): 907-24. PMID 3674018.
- Sakakibara M, Mukai T, Hori K (1985). "Nucleotide sequence of a cDNA clone for human aldolase: a messenger RNA in the liver. ". Biochem. Biophys. Res. Commun. 131 (1): 413-20. PMID 3840020.
- Ovádi J, Mohamed Osman IR, Batke J (1983). "Interaction of the dissociable glycerol-3-phosphate dehydrogenase and fructose-1,6-bisphosphate aldolase. Quantitative analysis by an extrinsic fluorescence probe. ". Eur. J. Biochem. 133 (2): 433-7. doi:10.1111/j.1432-1033.1983.tb07482.x. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document. PMID 6406231.
External links
Medical Subject Headings ( MeSH) is a huge Controlled vocabulary (or metadata system for the purpose of indexing journal articles and books This article is about the Enzyme Commission codes For the European Commission system for coding chemicals see EC-No. See also Gluconeogenesis, which carries out a process wherein glucose is synthesized rather than catabolized In Biochemistry, a metabolic pathway is a series of chemical reactions occurring within a cell. Glucose (Glc a Monosaccharide (or simple Sugar) also known as grape sugar, is an important Carbohydrate in Biology. Variation across species Hexokinases have been found in every organism checked ranging from bacteria, Yeast, and Plants to humans and other Vertebrates Glucose 6-phosphate (also known as Robison ester) is Glucose sugar Phosphorylated on carbon 6 Glucose-6-phosphate isomerase, or phosphoglucose isomerase, is an Enzyme ( that catalyzes the conversion of Glucose-6-phosphate into Fructose-6-phosphate Fructose 6-phosphate (also known as the Neuberg ester) is Fructose sugar Phosphorylated on carbon 6 (ie Phosphofructokinase-1 (PFK-1 is the most important regulatory Enzyme ( of Glycolysis. Fructose 16-phosphate is Fructose sugar Phosphorylated on carbons 1 and 6 (ie Aldolase A is an Enzyme which catalyses one of the Aldol reactions: The substrate, Fructose 16-bisphosphate (F-16-BP is broken down into Dihydroxyacetone phosphate (DHAP is a biochemical compound involved in many reactions from the Calvin cycle in plants to the ether-lipid biosynthesis process in Leishmania Glyceraldehyde 3-phosphate, also known as triose phosphate or 3-phosphoglyceraldehyde and abbreviated as G3P, GADP, GAP or PGAL Triose-phosphate isomerase (TPI or TIM is an Enzyme ( that catalyzes the reversible interconversion of the Triose phosphate Isomers Glyceraldehyde 3-phosphate, also known as triose phosphate or 3-phosphoglyceraldehyde and abbreviated as G3P, GADP, GAP or PGAL Glyceraldehyde 3-phosphate dehydrogenase (abbreviated as GAPDH or less commonly as G3PDH ( is an Enzyme that catalyzes the sixth step of Overview Phosphoglycerate mutase (PGM is an Enzyme that catalyzes step 8 of Glycolysis. In Enzymology, a phosphopyruvate hydratase ( is an Enzyme that catalyzes the Chemical reaction 2-phospho-D-glycerate \rightleftharpoons Enolase also known as phosphopyruvate dehydratase is a Metalloenzyme responsible for the catalysis of 2-phosphoglycerate (2-PG to Phosphoenolpyruvate (PEP Phosphoenolpyruvate (synonyms phosphoenolpyruvic acid, PEP) is an important Chemical compound in Biochemistry. Reaction The reaction with pyruvate kinase pyruvate kinase PEP ----------> pyruvate / \ ADP ATP Pyruvic acid (CH3COCO2H is an alpha-keto acid. The Carboxylate Anion of pyruvic acid is known as pyruvate. Pyruvate dehydrogenase (E1 is the first component Enzyme of Pyruvate dehydrogenase complex (PDC Acetyl-CoA is an important molecule in metabolism used in many biochemical reactions Coenzyme A ( CoA, CoASH, or HSCoA) is a Coenzyme, notable for its role in the synthesis and oxidation of Fatty acids
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