EC 184.108.40.206 Enzyme
Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
Hydrolysis of the alpha-D-mannosyl-(1->6)-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl sequence of glycoprotein to alpha-D-mannosyl-(1->6)-D-mannose and N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl sequences
The substrate group is a substituent on N-4 of an asparagine residue in the glycoprotein. The mannose residue at the non-reducing end of the sequence may carry further alpha-D-mannosyl groups on O-3 or O-6, but such a substituent on O-3 of the beta-D-mannosyl group prevents the action of the enzyme. The enzyme was obtained from the lily, Lilium longiflorum.
EC 220.127.116.11 created 2005
Ishimizu T, Sasaki A, Okutani S, Maeda M, Yamagishi M, Hase S.
Endo-beta-mannosidase, a plant enzyme acting on N-glycan: purification, molecular cloning, and characterization.
J. Biol. Chem. 279 (2004) 38555-62.
Sasaki A, Yamagishi M, Mega T, Norioka S, Natsuka S, Hase S.
Partial purification and characterization of a novel endo-beta-mannosidase acting on N-linked sugar chains from Lilium longflorum thumb.
J. Biochem. (Tokyo). 125 (1999) 363-7.
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