Chondroitinase is a 522 amino acid protein that localizes to the lysosome and functions as an exohydrolase that is essential for the degradation of glycosaminoglycans, keratan sulfate and chondroitin 6-sulfate. Using calcium as a cofactor, Chondroitinase, which exists as a disulfide linked oligomer, catalyzes the hydrolysis of the 6-sulfate group on target substrates. Defects in the gene encoding Chondroitinase are the cause of mucopolysaccharidosis type 4A (MPS4A), an autosomal recessive lysosomal storage disease that is characterized by the intracellular accumulation of keratan sulfate and chondroitin-6-sulfate and is associated with dental anomalies, short stature and, in some cases, death in the second or third decade of life.
