Activating Compound | Comment | Organism | Structure |
---|---|---|---|
Triton X-100 | activation, maximal at 0.5% Triton X-100 | Bos taurus | |
Triton X-100 | several-fold activation | Bos taurus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
1-deoxynojirimycin | 0.01 mM: 80% inhibition; strong inhibition | Bos taurus | |
additional information | no inhibition by conduritol B epoxide, bromoconduritols a and B, acarbose at 1 mM | Bos taurus | |
Nojirimycin | strong inhibition, 0.1 mM: 40% inhibition, 0.16 mM: 50% inhibition | Bos taurus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
endoplasmic reticulum | rough endoplasmic reticulum | Bos taurus | 5783 | - |
membrane | membrane-bound | Bos taurus | 16020 | - |
microsome | - |
Bos taurus | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
Glc3Man9GlcNAc2 + H2O | Bos taurus | hydrolyses specifically terminal alpha1,2-linked glucose residue | ? | - |
? | |
additional information | Bos taurus | involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins | ? | - |
? | |
additional information | Bos taurus | involved in processing of asparagine-linked oligosaccharides | ? | - |
? | |
additional information | Bos taurus | glucosidase I is a control enzyme for the regulation of glycoprotein processing | ? | - |
? | |
additional information | Bos taurus | involved in the formation of high mannose and complex glycoproteins | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bos taurus | - |
calf | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
Glc3Man9GlcNAc2-[protein] + H2O = Glc2Man9GlcNAc2-[protein] + beta-D-glucopyranose | glucosidase I is a specific alpha-(1,2)-glucosidase | Bos taurus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
liver | calf | Bos taurus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Glc3Man9GlcNAc2 + H2O | hydrolyses specifically terminal alpha1,2-linked glucose residue | Bos taurus | D-glucose + Glc2Man9GlcNAc2 | - |
? | |
Glc3Man9GlcNAc2 + H2O | hydrolyses specifically terminal alpha1,2-linked glucose residue | Bos taurus | ? | - |
? | |
Glc3Man9GlcNAc2-lipid + H2O | no significant difference in enzyme activity towards free, peptide-bound, or lipid-linked oligosaccharide, lipid- and peptide-linked oligosaccharide are hydrolyzed at a rate only 10% lower than free oligosaccharide | Bos taurus | D-glucose + Glc2Man9GlcNAc2-lipid | - |
? | |
Glc3Man9GlcNAc2-peptide + H2O | no significant difference in enzyme activity towards free, peptide-bound, or lipid-linked oligosaccharide, lipid- and peptide-linked oligosaccharide are hydrolyzed at a rate only 10% lower than free oligosaccharide | Bos taurus | D-glucose + Glc2Man9GlcNAc2-peptide | - |
? | |
additional information | involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins | Bos taurus | ? | - |
? | |
additional information | involved in processing of asparagine-linked oligosaccharides | Bos taurus | ? | - |
? | |
additional information | glucosidase I is a control enzyme for the regulation of glycoprotein processing | Bos taurus | ? | - |
? | |
additional information | involved in the formation of high mannose and complex glycoproteins | Bos taurus | ? | - |
? |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.2 | - |
- |
Bos taurus |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.16 | - |
Nojirimycin | - |
Bos taurus |