Chondroitin sulfate ABC lyase (ChABC)

Chondroitin sulfate ABC lyase (commonly known as chondroitinase ABC) is a bacterial enzyme, most extensively studied from *Proteus vulgaris*, that depolymerizes chondroitin sulfate, dermatan sulfate, and related glycosaminoglycans by cleaving their β-1,4-glycosidic bonds through β-elimination[1][3][4][8]. This degradation releases disaccharides and significantly reduces the inhibitory properties of these complex polysaccharides in the extracellular matrix, particularly after central nervous system injury, where chondroitin sulfate proteoglycans form a barrier to axonal regeneration[7][8]. Chondroitinase ABC exists in at least two closely related isoforms (chondroitinase ABC I and II), each with broad substrate specificities and distinct enzymatic properties[1][3][5]. The enzyme forms a ~120 kDa protein and consists of multiple structural domains that coordinate binding and catalysis of glycosaminoglycan substrates[2][3][4][5]. In research and developing clinical applications, chondroitinase ABC has shown promise in facilitating functional recovery following spinal cord injury by promoting neural regeneration and plasticity, but immunogenicity and delivery challenges remain major hurdles for therapeutic use[7][8][9]. There are no approved small molecule drugs that specifically interact with chondroitinase; rather, the enzyme itself is being studied as a therapeutic biological agent.

Other names

Chondroitinase ABCChondroitin ABC lyaseChondroitin ABC lyase IcABC-IcABC-IIChondroitinaseChondroitinase ABC from Proteus vulgaris

Catalyzes the eliminative cleavage of the β-1,4-glycosidic bond of chondroitin sulfate and dermatan sulfate (and to some extent hyaluronan) via a β-elimination mechanism, producing disaccharide fragments that disrupt glycosaminoglycan-mediated inhibition in the extracellular matrix[1][3][4][5][9]. Reduction of glial scarring and promotion of neural plasticity in central nervous system injury