ALDOC Human

Aldolase C is primarily expressed in the brain, specifically in the hippocampus and Purkinje cells . It plays a crucial role in glycolysis, the metabolic pathway that converts glucose into pyruvate, releasing energy and producing intermediates for other metabolic processes . The enzyme catalyzes the reversible aldol cleavage of fructose-1,6-bisphosphate and fructose 1-phosphate into dihydroxyacetone phosphate and either glyceraldehyde-3-phosphate or glyceraldehyde, respectively .

The ALDOC gene consists of 9 exons separated by 8 introns, similar to other aldolase genes in birds and mammals . The gene spans approximately 4 kilobases (kb) and includes one noncoding exon . The gene has been mapped to chromosome 17q11.2 .

The complete amino acid sequence of aldolase C was determined from recombinant genomic clones, revealing a polypeptide of 363 amino acids . Aldolase C shares 81% amino acid identity with aldolase A and 70% identity with aldolase B . The mRNA expression of ALDOC has been detected specifically in the brain .

Recombinant human aldolase C is produced using recombinant DNA technology, which involves inserting the ALDOC gene into a suitable expression system, such as bacteria or yeast, to produce the enzyme in large quantities . This recombinant enzyme is used in various research applications, including studies on glycolysis, brain metabolism, and related disorders .

Mutations or dysregulation of the ALDOC gene can be associated with certain metabolic disorders. For example, congenital disorders of glycosylation, type In, have been linked to abnormalities in aldolase C . Understanding the function and regulation of aldolase C is essential for developing potential therapeutic strategies for these conditions.