The enzyme mannuronate-specific alginate lyase (EC 4.2.2.3, formerly called poly(β-D-mannuronate) lyase) catalyzes the degradation of alginate into various monosaccharide and polysaccharide products:
- Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-α-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and β-D-mannuronate at their reducing end.
Quick Facts Identifiers, EC no. ...
Close
Quick Facts Alginate_lyase2, Identifiers ...
Close
Quick Facts Alginate_lyase, Identifiers ...
Close
Alginate lyase cleaves the glycosidic bonds of alginate via a β-elimination mechanism, in which it first converts alginate into several oligosaccharides containing unsaturated uronic acids at their non-reducing ends. It then cleaves the oligosaccharides, forming 4-deosy-L-erythro-5-hexoseulose uronic acid.[1]
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is alginate β-D-mannuronate—uronate lyase. Other names in common use include alginate lyase I, alginate lyase, alginase I, alginase II, and alginase. This enzyme participates in fructose and mannose metabolism.