Aldolase A

Aldolase A is an is_associated_with::enzyme that catalyses a reversible is_associated_with::aldol reaction: The substrate, is_associated_with::fructose 1,6-bisphosphate (F-1,6-BP) is broken down into is_associated_with::glyceraldehyde 3-phosphate and is_associated_with::dihydroxyacetone phosphate (is_associated_with::DHAP). This reaction is a part of is_associated_with::glycolysis. Three is_associated_with::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.

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 catalytic is_associated_with::amino acid residues involved in the reaction are is_associated_with::lysine and is_associated_with::tyrosine. The tyrosine acts as an efficient hydrogen acceptor while the lysine covalently binds and stabilizes the intermediates. Many is_associated_with::bacteria use two is_associated_with::magnesium is_associated_with::ions in place of the lysine.

Interactions
Aldolase A has been shown to interact with is_associated_with::PLD2.