Aldolase A is an enzyme that catalyses a reversible aldol reaction: The substrate, fructose 1,6-bisphosphate (F-1,6-BP) is broken down into glyceraldehyde 3-phosphate and dihydroxyacetone phosphate (DHAP). This reaction is a part of glycolysis. Three fructose-bisphosphate 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 that encode the same protein.
In mammalian aldolase, the key catalytic amino acid residues involved in the reaction are lysine and tyrosine. The tyrosine acts as an efficient hydrogen acceptor while the lysine covalently binds and stabilizes the intermediates. Many bacteria use two magnesiumions in place of the lysine.
The reaction mechanism of aldolase.
The enzyme's reactive site amino acid's side-chains are shown in blue.
^Kim, Jong Hyun; Lee Sukmook; Kim Jung Hwan; Lee Taehoon G; Hirata Masato; Suh Pann-Ghill; Ryu Sung Ho (Mar 2002). "Phospholipase D2 directly interacts with aldolase via Its PH domain". Biochemistry (United States) 41 (10): 3414–21. doi:10.1021/bi015700a. ISSN0006-2960. PMID11876650.
Pfleiderer G, Thöner M, Wachsmuth ED (1976). "Histological examination of the aldolase monomer composition of cells from human kidney and hypernephroid carcinoma". Beiträge zur Pathologie156 (3): 266–79. doi:10.1016/s0005-8165(75)80166-1. PMID766744.
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. doi:10.1515/bchm2.1977.358.1.169. PMID844801.
Wachsmuth ED (1976). "Differentiation of epithelial cells in human jejunum: localization and quantification of aminopeptidase, alkaline phosphatase and aldolase isozymes in tissue sections". Histochemistry48 (2): 101–9. doi:10.1007/BF00494548. PMID955981.
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. Acta1136 (1): 12–6. doi:10.1016/0167-4889(92)90078-P. PMID1353685.
Vértessy BG, Orosz F, Ovádi J (1991). "Modulation of the interaction between aldolase and glycerol-phosphate dehydrogenase by fructose phosphates". Biochim. Biophys. Acta1078 (2): 236–42. doi:10.1016/0167-4838(91)90564-g. PMID2065091.
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. PMID2229018.
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. PMID3391172.
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. PMID3441006.
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. PMID3570299.
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. doi:10.1016/0006-291X(85)91818-2. PMID3840020.
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. PMID6406231.