EC 3.2.1.107 - Protein-glucosylgalactosylhydroxylysine glucosidase

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IntEnz Enzyme Nomenclature
EC 3.2.1.107

Names

Accepted name:
protein-glucosylgalactosylhydroxylysine glucosidase
Other names:
2-O-α-D-glucopyranosyl-5-O-α-D-galactopyranosylhydroxy-L-lysine glucohydrolase
protein-α-D-glucosyl-1,2-β-D-galactosyl-L-hydroxylysine glucohydrolase
protein-α-D-glucosyl-(1→2)-β-D-galactosyl-L-hydroxylysine glucohydrolase
PGGHG (gene name)
Systematic name:
[collagen]-(5R)-5-O-[α-D-glucosyl-(1→2)-β-D-galactosyl]-5-hydroxy-L-lysine glucohydrolase

Reaction

Comments:

The enzyme specifically hydrolyses glucose from α-D-glucosyl-(1→2)-β-D-galactosyl disaccharide units that are linked to hydroxylysine residues of collagen and collagen-like proteins. Acetylation of the ε-amino group of the glycosylated hydroxylysine abolishes activity.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0047402
CAS Registry Number: 72829-45-9
UniProtKB/Swiss-Prot:

References

  1. Hamazaki, H. and Hotta, K.
    Purification and characterization of an α-glucosidase specific for hydroxylysine-linked disaccharide of collagen.
    J. Biol. Chem. 254: 9682-9687 (1979). [PMID: 385589]
  2. Hamazaki, H. and Hotta, K.
    Enzymatic hydrolysis of disaccharide unit of collagen. Isolation of 2-O-α-D-glucopyranosyl-O-β-D-galactopyranosyl-hydroxylysine glucohydrolase from rat spleens.
    Eur. J. Biochem. 111: 587-591 (1980). [PMID: 7460918]
  3. Sternberg, M. and Shapiro, R.G.
    Studies on the catabolism of the hydroxylysine-linked disaccharide units of basement membranes and collagens. Isolation and characterization of a rat kidney α-glucosidase of high specificity.
    J. Biol. Chem. 254: 10329-10336 (1979). [PMID: 385599]
  4. Hamazaki, H., Hamazaki, M. H.
    Catalytic site of human protein-glucosylgalactosylhydroxylysine glucosidase: Three crucial carboxyl residues were determined by cloning and site-directed mutagenesis.
    Biochem. Biophys. Res. Commun. 469: 357-362 (2016). [PMID: 26682924]

[EC 3.2.1.107 created 1984]