Rhea - reaction knowledgebase

Enzymes

UniProtKB ^help_outline	5 proteins
Enzyme class ^help_outline	EC 3.2.1.107 protein-glucosylgalactosylhydroxylysine glucosidase
GO Molecular Function ^help_outline	GO:0047402 protein-glucosylgalactosylhydroxylysine glucosidase activity

Reaction participants Show >> << Hide

Name^help_outline (5R)-5-O-[α-D-glucosyl-(1→2)-β-D-galactosyl]-5-hydroxy-L-lysyl-[collagen] Identifier RHEA-COMP:12754 Reactive part ^help_outline
- Name ^help_outline (5R)-5-O-[α-D-glucosyl-(1→2)-β-D-galactosyl]-5-hydroxy-L-lysine residue Identifier CHEBI:133452 Charge 1 Formula C18H33N2O12 SMILES^help_outline [C@@H](C(*)=O)(CC[C@H](C[NH3+])O[C@@H]1O[C@@H]([C@@H]([C@@H]([C@H]1O[C@@H]2[C@@H]([C@H]([C@@H]([C@H](O2)CO)O)O)O)O)O)CO)N* 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Search links Involved in 2 reaction(s) Find proteins in UniProtKB for this molecule
Name ^help_outline H₂O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) ^help_outline Charge 0 Formula H2O InChIKey^help_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILES^help_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name^help_outline (5R)-5-O-(β-D-galactosyl)-5-hydroxy-L-lysyl-[collagen] Identifier RHEA-COMP:12753 Reactive part ^help_outline
- Name ^help_outline (5R)-5-O-(β-D-galactosyl)-5-hydroxy-L-lysine residue Identifier CHEBI:133443 Charge 1 Formula C12H23N2O7 SMILES^help_outline [C@@H](C(*)=O)(CC[C@H](C[NH3+])O[C@@H]1O[C@@H]([C@@H]([C@@H]([C@H]1O)O)O)CO)N* 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Search links Involved in 3 reaction(s) Find proteins in UniProtKB for this molecule
Name ^help_outline D-glucose Identifier CHEBI:4167 (Beilstein: 1281604; CAS: 2280-44-6) ^help_outline Charge 0 Formula C6H12O6 InChIKey^help_outline WQZGKKKJIJFFOK-GASJEMHNSA-N SMILES^help_outline OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 161 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule

Cross-references

	RHEA:11068	RHEA:11069	RHEA:11070	RHEA:11071
Reaction direction	undefined	left-to-right	right-to-left	bidirectional
UniProtKB ^help_outline	5 proteins
EC numbers ^help_outline	3.2.1.107
Gene Ontology ^help_outline	GO:0047402
KEGG ^help_outline				R04503
MetaCyc ^help_outline		3.2.1.107-RXN

Publications

Studies on the catabolism of the hydroxylysine-linked disaccharide units of basement membranes and collagens. Isolation and characterization of a rat kidney alpha-glucosidase of high specificity.

Sternberg M., Spiro R.G.

J Biol Chem 254:10329-10336(1979) [PubMed] [EuropePMC]
Catalytic site of human protein-glucosylgalactosylhydroxylysine glucosidase: Three crucial carboxyl residues were determined by cloning and site-directed mutagenesis.

Hamazaki H., Hamazaki M.H.

Protein-glucosylgalactosylhydroxylysine glucosidase (PGGHG; EC3.2.1.107) cleaves glucose from disaccharide unit (Glc-α1,2-Gal) linked to hydroxylysine residues of collagen. In the present paper we first show that PGGHG is the product of ATHL1 gene as follows. (1) PGGHG was purified from chick embr ... >> More

Protein-glucosylgalactosylhydroxylysine glucosidase (PGGHG; EC3.2.1.107) cleaves glucose from disaccharide unit (Glc-α1,2-Gal) linked to hydroxylysine residues of collagen. In the present paper we first show that PGGHG is the product of ATHL1 gene as follows. (1) PGGHG was purified from chick embryos and digested with trypsin. LC-MS/MS analysis suggested the tryptic-peptides were from the ATHL1 gene product. (2) Chick embryo ATHL1 cDNA was cloned to a cloning and expression vector and two plasmid clones with different ATHL1 CDS insert were obtained. (3) Each plasmid DNA was transformed into Escherichia coli cells for expression and two isoforms of chicken PGGHG were obtained. (4) Both isoforms effectively released glucose from type IV collagen. Next, we searched for carboxyl residues crucial for catalytic activity as follows; human ATHL1 cDNA was cloned into a cloning and expression vector and 18 mutants were obtained by site-directed mutagenesis for 15 carboxyl residues conserved in ATHL1 of jawed vertebrates. The expression analysis indicated that substitutions of Asp301, Glu430 and Glu574 with sterically conservative (D301N, E430Q, E574Q) or functionally conservative (D301E, E430D, E574D) residues led to the complete elimination of enzyme activity. These findings lead us to the conclusion that PGGHG is encoded by ATHL1 and three carboxyl residues (corresponding to Asp301, Glu430 and Glu574 of human PGGHG) might be involved in the catalytic site of PGGHG. << Less

Biochem. Biophys. Res. Commun. 469:357-362(2016) [PubMed] [EuropePMC]
Purification and characterization of an alpha-glucosidase specific for hydroxylysine-linked disaccharide of collagen.

Hamazaki H., Hotta K.

J Biol Chem 254:9682-9687(1979) [PubMed] [EuropePMC]
Enzymatic hydrolysis of disaccharide unit of collagen. Isolation of 2-O-alpha-D-glucopyranosyl-O-beta-D-galactopyranosyl-hydroxylysine glucohydrolase from rat spleens.

Hamazaki H., Hotta K.

The hydroxylsine-linked disaccharide unit, 2-O-alpha-D-glucopyranosyl-O-beta-D-galactopyranosyl-hydroxylysine (Glc-Gal-Hyl), prepared from collagens, was hydrolyzed by a glucohydrolase present in rat spleens and lungs. This disaccharide unit was scarcely hydrolyzed by homogenates of intestines, li ... >> More

The hydroxylsine-linked disaccharide unit, 2-O-alpha-D-glucopyranosyl-O-beta-D-galactopyranosyl-hydroxylysine (Glc-Gal-Hyl), prepared from collagens, was hydrolyzed by a glucohydrolase present in rat spleens and lungs. This disaccharide unit was scarcely hydrolyzed by homogenates of intestines, livers, and kidneys, which had a high alpha-D-glucosidase activity for neutral glucosides. The Glc-Gal-Hyl glucohydrolase was purified from rat spleens by affinity chromatography and gel filtration to the extent that sodium dodecyl sulfate/polyacrylamide gel electrophoresis gave a single band stained by Coomassie blue G-250. This purified glucohydrolase had a pH optimum around 5.8, and the Michaelis constant was 5.9 mM when Glc-Gal-Hyl was used as a substrate. This enzyme did not hydrolyze neutral glucosides. It is concluded that this Glc-Gal-Hyl glucohydrolase is responsible for catabolism of the hydroxylsine-linked disaccharide unit derived from collagens in mammals. << Less

Eur J Biochem 111:587-591(1980) [PubMed] [EuropePMC]

RHEA:11068 (5R)-5-O-[alpha-D-glucosyl-(1->2)-beta-D-galactosyl]-5-hydroxy-L-lysyl-[collagen] + H2O = (5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysyl-[collagen] + D-glucose

Enzymes

Reaction participants Show >> << Hide

Cross-references

Publications

Studies on the catabolism of the hydroxylysine-linked disaccharide units of basement membranes and collagens. Isolation and characterization of a rat kidney alpha-glucosidase of high specificity.

Catalytic site of human protein-glucosylgalactosylhydroxylysine glucosidase: Three crucial carboxyl residues were determined by cloning and site-directed mutagenesis.

Purification and characterization of an alpha-glucosidase specific for hydroxylysine-linked disaccharide of collagen.

Enzymatic hydrolysis of disaccharide unit of collagen. Isolation of 2-O-alpha-D-glucopyranosyl-O-beta-D-galactopyranosyl-hydroxylysine glucohydrolase from rat spleens.