EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.2.1.106 | 1-deoxynojirimycin | - |
Saccharomyces cerevisiae | |
3.2.1.106 | castanospermine | - |
Saccharomyces cerevisiae |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.2.1.106 | endoplasmic reticulum | - |
Saccharomyces cerevisiae | 5783 | - |
3.2.1.106 | membrane | membrane-bound | Saccharomyces cerevisiae | 16020 | - |
3.2.1.106 | membrane | type-II transmembrane protein | Saccharomyces cerevisiae | 16020 | - |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.2.1.106 | 97000 | - |
calculated from nucleotide sequence | Saccharomyces cerevisiae |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.106 | Glc3Man9GlcNAc2 + H2O | Saccharomyces cerevisiae | hydrolyses specifically terminal alpha1,2-linked glucose residue | ? | - |
? | |
3.2.1.106 | Glc3Man9GlcNAc2 + H2O | Saccharomyces cerevisiae | specific involvement in the N-linked oligosaccharide-processing pathway | ? | - |
? | |
3.2.1.106 | additional information | Saccharomyces cerevisiae | involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins | ? | - |
? | |
3.2.1.106 | additional information | Saccharomyces cerevisiae | cell wall 1,6-beta-glucan synthesis depends on endoplasmic reticulum glucosidase I and II, and the molecular chaperone BiP/Kar2p in a synergistic manner | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.106 | Saccharomyces cerevisiae | - |
- |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
3.2.1.106 | glycoprotein | - |
Saccharomyces cerevisiae |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.106 | alpha-D-Glc-(1-2)-alpha-D-Glc-(1-3)-alpha-D-Glc-O(CH2)8-COOCH3 + H2O | synthetic trisaccharide | Saccharomyces cerevisiae | beta-D-glucose + alpha-D-Glc-(1-3)-alpha-D-Glc-O(CH2)8-COOCH3 | - |
? | |
3.2.1.106 | Glc3Man9GlcNAc2 + H2O | hydrolyses specifically terminal alpha1,2-linked glucose residue | Saccharomyces cerevisiae | D-glucose + Glc2Man9GlcNAc2 | - |
? | |
3.2.1.106 | Glc3Man9GlcNAc2 + H2O | hydrolyses specifically terminal alpha1,2-linked glucose residue | Saccharomyces cerevisiae | ? | - |
? | |
3.2.1.106 | Glc3Man9GlcNAc2 + H2O | specific involvement in the N-linked oligosaccharide-processing pathway | Saccharomyces cerevisiae | ? | - |
? | |
3.2.1.106 | additional information | also acts, more slowly, on the corresponding glycolipids and glycopeptides | Saccharomyces cerevisiae | ? | - |
? | |
3.2.1.106 | additional information | aryl-alpha-D-glucosides: not a substrate | Saccharomyces cerevisiae | ? | - |
? | |
3.2.1.106 | additional information | involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins | Saccharomyces cerevisiae | ? | - |
? | |
3.2.1.106 | additional information | cell wall 1,6-beta-glucan synthesis depends on endoplasmic reticulum glucosidase I and II, and the molecular chaperone BiP/Kar2p in a synergistic manner | Saccharomyces cerevisiae | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.106 | CWH41 | - |
Saccharomyces cerevisiae |
3.2.1.106 | Cwh41p | Cwh41p is yeast glucosidase I | Saccharomyces cerevisiae |
3.2.1.106 | Cwh41p | CWH41 gene encodes glucosidase I | Saccharomyces cerevisiae |
3.2.1.106 | Cwh41p | calcofluor white hypersensitivity | Saccharomyces cerevisiae |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.106 | 37 | - |
assay at | Saccharomyces cerevisiae |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.106 | 6.8 | - |
assay at | Saccharomyces cerevisiae |