| EC |
3.2.1.107 |
| Accepted name: |
protein-glucosylgalactosylhydroxylysine glucosidase |
| Reaction: |
[collagen]-(5R)-5-O-[α-D-glucosyl-(1→2)-β-D-galactosyl]-5-hydroxy-L-lysine + H2O = D-glucose + [collagen]-(5R)-5-O-(β-D-galactosyl)-5-hydroxy-L-lysine |
| Other name(s): |
PGGHG (gene name); 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 |
| Systematic name: |
[collagen]-(5R)-5-O-[α-D-glucosyl-(1→2)-β-D-galactosyl]-5-hydroxy-L-lysine glucohydrolase |
| 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: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 72829-45-9 |
| 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 (1979) 9682–9687. [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 (1980) 587–591. [DOI] [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 (1979) 10329–10336. [PMID: 385599] |
| 4. |
Hamazaki, H. and 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 (2016) 357–362. [DOI] [PMID: 26682924] |
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| [EC 3.2.1.107 created 1984] |
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