Dental enamel is a highly mineralized tissue with 85% of its volume occupied by unusually large, highly organized, hydroxyapatite crystals. This highly organized and unusual structure is thought to be rigorously controlled in ameloblasts through the interaction of a number of organic matrix molecules that include enamelin, amelogenin (AMELX), ameloblastin (AMBN), tuftelin, dentine sialophosphoprotein (DSPP), and a variety of enzymes.

Enamelin is the largest protein in the enamel matrix of developing teeth and comprises approximately 5% of total enamel matrix protein.The current description of enamelin is a protein coded at 4q13.3 and is a modulator for mineral formation and crystal elongation in enamel. Significant proteins in enamel are amelogenins and ameloblastins.