Enzymes
| UniProtKB help_outline | 2 proteins |
Reaction participants Show >> << Hide
- Name help_outline β-D-Gal-(1→3)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-D-Glc Identifier CHEBI:30248 Charge 0 Formula C26H45NO21 InChIKeyhelp_outline AXQLFFDZXPOFPO-FSGZUBPKSA-N SMILEShelp_outline CC(=O)N[C@H]1[C@H](O[C@H]2[C@@H](O)[C@@H](CO)O[C@@H](O[C@H]3[C@H](O)[C@@H](O)C(O)O[C@@H]3CO)[C@@H]2O)O[C@H](CO)[C@@H](O)[C@@H]1O[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,485 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline β-D-galactosyl-(1→3)-N-acetyl-D-glucosamine Identifier CHEBI:27707 (Beilstein: 1356092) help_outline Charge 0 Formula C14H25NO11 InChIKeyhelp_outline HMQPEDMEOBLSQB-RPHKZZMBSA-N SMILEShelp_outline [C@@H]1(O)[C@H](O)[C@H]([C@H](O[C@@H]2[C@H](C(O[C@@H]([C@H]2O)CO)O)NC(C)=O)O[C@@H]1CO)O 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline lactose Identifier CHEBI:17716 (CAS: 63-42-3) help_outline Charge 0 Formula C12H22O11 InChIKeyhelp_outline GUBGYTABKSRVRQ-QKKXKWKRSA-N SMILEShelp_outline OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 12 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:21568 | RHEA:21569 | RHEA:21570 | RHEA:21571 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
|||
| EC numbers help_outline | ||||
| Gene Ontology help_outline | ||||
| KEGG help_outline | ||||
| MetaCyc help_outline |
Publications
-
An enzyme releasing lacto-N-biose from oligosaccharides.
Sano M., Hayakawa K., Kato I.
alpha-L-Fucosidase (alpha-L-fucoside fucohydrolase; EC 3.2.1.51) preparations from Streptomyces sp. 142 were found to contain an enzyme specific for lacto-N-biosidic (Gal beta 1-3GlcNAc beta 1-) linkages (type 1 structure) in oligosaccharides. The enzyme preparation, which was eluted after alpha-f ... >> More
alpha-L-Fucosidase (alpha-L-fucoside fucohydrolase; EC 3.2.1.51) preparations from Streptomyces sp. 142 were found to contain an enzyme specific for lacto-N-biosidic (Gal beta 1-3GlcNAc beta 1-) linkages (type 1 structure) in oligosaccharides. The enzyme preparation, which was eluted after alpha-fucosidase from a CM-Sepharose column, contained some alpha-fucosidase activity but was free from other glycosidases and proteases. Substrate specificity studies with oligosaccharides labeled with 2-aminopyridine showed that the enzyme specifically hydrolyzed lacto-N-tetraose (Gal beta 1-3GlcNAc beta 1-3Gal beta 1-4Glc) but did not hydrolyze lacto-N-neotetraose (Gal beta 1-4GlcNAc beta 1-3Gal beta 1-4Glc), lacto-N-triose, sialyl lacto-N-tetraose, lacto-N-fucopentaose I, II, or III, asialo-GM1 tetrasaccharide, or poly-N-acetyllactosamine. Structural analysis of the enzyme digest of the N-acetyllactosamine type of triantennary sugar chain with type 1 structure showed that lacto-N-biose (Gal beta 1-3GlcNAc) and the N-acetyllactosamine type of biantennary sugar chain were produced. Thus this enzyme was tentatively named lacto-N-biosidase, because it hydrolyzes oligosaccharides containing a type 1 structure at the nonreducing terminus and produces lacto-N-biose. << Less
Proc Natl Acad Sci U S A 89:8512-8516(1992) [PubMed] [EuropePMC]
-
Purification and characterization of an enzyme releasing lacto-N-biose from oligosaccharides with type 1 chain.
Sano M., Hayakawa K., Kato I.
An enzyme specific for oligosaccharides with type 1 chain was purified 7,000-fold from the culture broth of Streptomyces sp. 142. The enzyme, lacto-N-biosidase, was induced and secreted into culture medium when the strain was cultured in the presence of porcine stomach mucin. The enzyme was purifi ... >> More
An enzyme specific for oligosaccharides with type 1 chain was purified 7,000-fold from the culture broth of Streptomyces sp. 142. The enzyme, lacto-N-biosidase, was induced and secreted into culture medium when the strain was cultured in the presence of porcine stomach mucin. The enzyme was purified by anion-exchange chromatography on Q Sepharose, cation-exchange chromatography on S Sepharose, fast protein liquid chromatography on a Mono S column, and gel filtration chromatography on TSK gel HW55S. To remove contaminating alpha-1,3/4-fucosidase and beta-N-acetylglucosaminidase, final purification was done by fast protein liquid chromatography on a Mono S column and affinity chromatography on N-acetylglucosamine agarose. The purified enzyme gave only one major protein band with an apparent M(r) of 60,000 on sodium dodesyl sulfate-polyacrylamide gel electrophoresis. The enzyme had maximum activity at pH 5.5 and was stable at the pH range of 4.0-10.0. Substrate specificity studies with oligosaccharides labeled with 2-aminopyridine showed that the enzyme specifically hydrolyzed lacto-N-tetraose and the N-acetyllactosamine type of triantennary sugar chain with the type 1 chain, but did not hydrolyze type 2 chain oligosaccharides or the type 1 chain oligosaccharides with fucose or sialic acid including lacto-N-fucopentaose I and II and alpha-2,3-sialyl lacto-N-tetraose. The enzyme released lacto-N-biose from asialofetuin, and almost all oligosaccharides in asialofetuin were found to have only type 2 chains. Sequential digestion of extended type 1 chain oligosaccharides with alpha-1,3/4-fucosidase and lacto-N-biosidase was possible. << Less