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Literature summary extracted from

  • Szumilo, T.; Kaushal, G.P.; Elbein, A.D.
    Purification and properties of glucosidase I from mung bean seedlings (1986), Arch. Biochem. Biophys., 247, 261-271.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.1.106 Triton X-100 0.2% Triton X-100: 4 to 5fold activation, glucosidase I releases in a soluble form by treating microsomal particles with 1.5% Triton X-100, not an absolute requirement for Triton X-100 Vigna radiata

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.106 1-deoxynojirimycin strong inhibition Vigna radiata
3.2.1.106 2,5-Dihydroxymethyl-3,4-dihydroxypyrrolidine plant pyrrolidine alkaloid, DMDP, 0.04 mM: 50% inhibition Vigna radiata
3.2.1.106 castanospermine plant indolizidine alkaloid, strong inhibition Vigna radiata
3.2.1.106 chloride inhibitory above 0.3 M, 0.5 M: 30% inhibition Vigna radiata
3.2.1.106 Co2+ quite inhibitory Vigna radiata
3.2.1.106 Cu2+ quite inhibitory Vigna radiata
3.2.1.106 ethanolamine
-
Vigna radiata
3.2.1.106 glycerol 2% or higher: 25% or more inhibition Vigna radiata
3.2.1.106 kojibiose 0.5 mM: 50% inhibition; alpha-1,2-linked glucose disaccharide Vigna radiata
3.2.1.106 additional information no inhibition by alpha-1,3-, alpha-1,4-, and alpha-1,6-linked glucose disaccharides; no inhibition by EDTA; no inhibition by nigerose, maltose, isomaltose at 2 mM; no inhibition by swainsonine, deoxymannojirimycin or 1,4-dideoxy-1,4-imino-D-mannitol Vigna radiata
3.2.1.106 phosphate inhibitory above 0.3 M, 0.5 M: 30% inhibition Vigna radiata
3.2.1.106 sulfate 0.1-0.2 M: 15-20% inhibition, somewhate more inhibitory at higher concentrations Vigna radiata
3.2.1.106 tricine
-
Vigna radiata
3.2.1.106 Tris 20 mM: 50% inhibition Vigna radiata
3.2.1.106 Zn2+ quite inhibitory Vigna radiata

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.106 endoplasmic reticulum
-
Vigna radiata 5783
-
3.2.1.106 membrane membrane-bound Vigna radiata 16020
-
3.2.1.106 microsome
-
Vigna radiata
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.106 additional information no requirement for divalent cations Vigna radiata

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.106 316000
-
gel fitration Vigna radiata

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.106 Glc3Man9GlcNAc2 + H2O Vigna radiata hydrolyses specifically terminal alpha1,2-linked glucose residue ?
-
?
3.2.1.106 Glc3Man9GlcNAc2 + H2O Vigna radiata specific involvement in the N-linked oligosaccharide-processing pathway ?
-
?
3.2.1.106 Glc3Man9GlcNAc2 + H2O Vigna radiata involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins ?
-
?
3.2.1.106 Glc3Man9GlcNAc2 + H2O Vigna radiata involved in processing of asparagine-linked oligosaccharides ?
-
?
3.2.1.106 additional information Vigna radiata involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins ?
-
?
3.2.1.106 additional information Vigna radiata involved in processing of asparagine-linked oligosaccharides ?
-
?
3.2.1.106 additional information Vigna radiata first enzyme of processing of N-linked oligosaccharides in plants, plant glucosidase I might be analogous to glucosidase I of animal cells ?
-
?
3.2.1.106 additional information Vigna radiata involved in the formation of high mannose and complex glycoproteins ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.106 Vigna radiata
-
mung bean
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.106 glycoprotein with high-mannose oligosaccharides Vigna radiata

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.106
-
Vigna radiata

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.106 Glc3Man9GlcNAc2-[protein] + H2O = Glc2Man9GlcNAc2-[protein] + beta-D-glucopyranose glucosidase I is a specific alpha-(1,2)-glucosidase Vigna radiata

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.106 seedling
-
Vigna radiata
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.106 additional information
-
-
Vigna radiata

Storage Stability

EC Number Storage Stability Organism
3.2.1.106 -18°C, 10% glycerol, few weeks, no loss of activity Vigna radiata
3.2.1.106 0°C, very slight loss of activity Vigna radiata
3.2.1.106 27°C, 40 h, more than 50% activity retained Vigna radiata
3.2.1.106 37°C, most of activity lost during storage Vigna radiata

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.106 Glc3Man9GlcNAc + H2O hydrolyses specifically terminal alpha1,2-linked glucose residue Vigna radiata D-glucose + Glc2Man9GlcNAc
-
?
3.2.1.106 Glc3Man9GlcNAc2 + H2O hydrolyses specifically terminal alpha1,2-linked glucose residue Vigna radiata D-glucose + Glc2Man9GlcNAc2
-
?
3.2.1.106 Glc3Man9GlcNAc2 + H2O hydrolyses specifically terminal alpha1,2-linked glucose residue Vigna radiata ?
-
?
3.2.1.106 Glc3Man9GlcNAc2 + H2O specific involvement in the N-linked oligosaccharide-processing pathway Vigna radiata ?
-
?
3.2.1.106 Glc3Man9GlcNAc2 + H2O involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins Vigna radiata ?
-
?
3.2.1.106 Glc3Man9GlcNAc2 + H2O involved in processing of asparagine-linked oligosaccharides Vigna radiata ?
-
?
3.2.1.106 Glc3Man9GlcNAc2-lipid + H2O hydrolyses specifically terminal alpha1,2-linked glucose residue Vigna radiata D-glucose + Glc2Man9GlcNAc2-lipid
-
?
3.2.1.106 Glc3Man9GlcNAc2-peptide + H2O hydrolyses specifically terminal alpha1,2-linked glucose residue Vigna radiata D-glucose + Glc2Man9GlcNAc2-peptide
-
?
3.2.1.106 additional information Glc1Man9GlcNAc2: not a substrate Vigna radiata ?
-
?
3.2.1.106 additional information also acts, more slowly, on the corresponding glycolipids and glycopeptides Vigna radiata ?
-
?
3.2.1.106 additional information p-nitrophenyl-alpha-D-glucopyranoside: not a substrate Vigna radiata ?
-
?
3.2.1.106 additional information Glc2Man9GlcNAc2: not a substrate Vigna radiata ?
-
?
3.2.1.106 additional information substrate and product specificity Vigna radiata ?
-
?
3.2.1.106 additional information involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins Vigna radiata ?
-
?
3.2.1.106 additional information involved in processing of asparagine-linked oligosaccharides Vigna radiata ?
-
?
3.2.1.106 additional information first enzyme of processing of N-linked oligosaccharides in plants, plant glucosidase I might be analogous to glucosidase I of animal cells Vigna radiata ?
-
?
3.2.1.106 additional information involved in the formation of high mannose and complex glycoproteins Vigna radiata ?
-
?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.106 27
-
40 h: 50% activity retained Vigna radiata
3.2.1.106 37
-
most activity lost during storage Vigna radiata

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.106 6.3 6.5
-
Vigna radiata

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.106 5.5 6.8 activity greatly decreases at pH values below 5.5 or above 6.8 Vigna radiata

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.106 6.5 7 most stable at Vigna radiata

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.2.1.106 0.04
-
2,5-Dihydroxymethyl-3,4-dihydroxypyrrolidine plant pyrrolidine alkaloid, DMDP Vigna radiata
3.2.1.106 0.5
-
kojibiose
-
Vigna radiata