Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.2.1.106 extracted from

  • Schweden, J.; Borgmann, C.; Legler, G.; Bause, E.
    Characterization of calf liver glucosidase I and its inhibition by basic sugar analogs (1986), Arch. Biochem. Biophys., 248, 335-340.
    View publication on PubMed
Search for more literature for 3.2.1.106

Inhibitors

Inhibitors Comment Organism Structure
1-deoxymannojirimycin very slight inhibition, Ki = 0.19 mM Bos taurus
1-deoxynojirimycin strong inhibition; strong inhibition, Ki = 0.0001 mM Bos taurus
additional information inhibition of glucosidase I as a function of pH, pH dependence of inhibition, the inhibiting species is the cationic form of the inhibitor; no inhibition by EDTA Bos taurus
N,N-dimethyl-1-deoxynojirimycin strong inhibition; strong inhibition, Ki = 0.0004 mM Bos taurus
N-(5-carboxypentyl)-1-deoxynojirimycin strong inhibition; strong inhibition, Ki = 0.0005 mM Bos taurus
N-5-carboxypentyl-1-deoxymannojirimycin very slight inhibition, Ki = 0.1 mM Bos taurus
N-butyl-1-deoxynojirimycin strong inhibition, Ki = 0.00009 mM Bos taurus
N-decanoyl-1-deoxynojirimycin very slight inhibition, Ki = 0.07 mM Bos taurus
N-decyl-1-deoxynojirimycin strong inhibition, Ki = 0.0004 mM Bos taurus
N-hexyl-1-deoxynojirimycin strong inhibition, Ki = 0.00013 mM Bos taurus
N-methyl-1-deoxymannojirimycin very slight inhibition, Ki = 0.017 mM Bos taurus
N-methyl-1-deoxynojirimycin strong inhibition; strong inhibition, Ki = 0.00007 mM Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic data Bos taurus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Bos taurus 16020
-
microsome
-
 Bos taurus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
additional information metal ions not required Bos taurus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
83000
-
 calf, 2 * 83000, formation of tetramers and dimers, SDS-PAGE Bos taurus
83000
-
 calf, 4 * 83000, formation of tetramers and dimers, SDS-PAGE Bos taurus
150000 170000 calf, gel filtration Bos taurus
320000 350000 calf, gel filtration Bos taurus

Natural Substrates/ Products (Substrates)

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 ?
-
 ?
Glc3Man9GlcNAc2 + H2O Bos taurus specific involvement in the N-linked oligosaccharide-processing pathway ?
-
 ?
Glc3Man9GlcNAc2 + H2O Bos taurus involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins ?
-
 ?
Glc3Man9GlcNAc2 + H2O Bos taurus involved in processing of asparagine-linked oligosaccharides ?
-
 ?
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 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Bos taurus
-
 calf
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein with high-mannose oligosaccharides Bos taurus

Purification (Commentary)

Purification (Comment) Organism
calf Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
liver calf Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Glc3Man5GlcNAc + H2O hydrolyses specifically terminal alpha1,2-linked glucose residue Bos taurus D-glucose + Glc2Man5GlcNAc
-
 ?
Glc3Man5GlcNAc + H2O hydrolyzed at a rate similar to that of natural substrate Glc3Man9GlcNAc2 Bos taurus D-glucose + Glc2Man5GlcNAc
-
 ?
Glc3Man6GlcNAc + H2O hydrolyses specifically terminal alpha1,2-linked glucose residue Bos taurus D-glucose + Glc2Man6GlcNAc
-
 ?
Glc3Man6GlcNAc + H2O slowly hydrolyzed Bos taurus D-glucose + Glc2Man6GlcNAc
-
 ?
Glc3Man7GlcNAc + H2O hydrolyses specifically terminal alpha1,2-linked glucose residue Bos taurus D-glucose + Glc2Man7GlcNAc
-
 ?
Glc3Man7GlcNAc + H2O slowly hydrolyzed Bos taurus D-glucose + Glc2Man7GlcNAc
-
 ?
Glc3Man8GlcNAc + H2O hydrolyses specifically terminal alpha1,2-linked glucose residue Bos taurus D-glucose + Glc2Man8GlcNAc
-
 ?
Glc3Man8GlcNAc + H2O slowly hydrolyzed Bos taurus D-glucose + Glc2Man8GlcNAc
-
 ?
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 + H2O specific involvement in the N-linked oligosaccharide-processing pathway Bos taurus ?
-
 ?
Glc3Man9GlcNAc2 + H2O involved in first step of processing of oligosaccharides after transfer from dolichyl diphosphate to proteins Bos taurus ?
-
 ?
Glc3Man9GlcNAc2 + H2O involved in processing of asparagine-linked oligosaccharides Bos taurus ?
-
 ?
Glc3Man9GlcNAc2-lipid + H2O slowly hydrolyzed, free and peptide-bound Glc3Man9GlcNAc2 oligosaccharides are hydrolyzed at similar rates, both being about threefold better substrates than the lipid-linked structure Bos taurus D-glucose + Glc2Man9GlcNAc2-lipid
-
 ?
Glc3Man9GlcNAc2-peptide + H2O free and peptide-bound Glc3Man9GlcNAc2 oligosaccharides are hydrolyzed at similar rates, both being about threefold better substrates than the lipid-linked structure Bos taurus D-glucose + Glc2Man9GlcNAc2-peptide
-
 ?
additional information Glc1Man9GlcNAc2: not a substrate Bos taurus ?
-
 ?
additional information also acts, more slowly, on the corresponding glycolipids and glycopeptides Bos taurus ?
-
 ?
additional information structure of the Glc3 branch rather than the more distant domains of the oligosaccharide molecule are controlling specificity Bos taurus ?
-
 ?
additional information Glc2Man9GlcNAc2: not a substrate Bos taurus ?
-
 ?
additional information substrate specificities Bos taurus ?
-
 ?
additional information p-nitrophenyl-glucosides: no substrates Bos taurus ?
-
 ?
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 ?
-
 ?

Subunits

Subunits Comment Organism
dimer calf, 2 * 83000, formation of tetramers and dimers, SDS-PAGE Bos taurus
tetramer calf, 4 * 83000, formation of tetramers and dimers, SDS-PAGE Bos taurus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Bos taurus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.7
-
 calf Bos taurus
6.7
-
 sharp maximum close to Bos taurus

pH Range

pH Minimum pH Maximum Comment Organism
5.8 7.4 half-maximal activity Bos taurus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00007
-
 N-methyl-1-deoxynojirimycin
-
 Bos taurus
0.00009
-
 N-butyl-1-deoxynojirimycin strong inhibition Bos taurus
0.00013
-
 N-hexyl-1-deoxynojirimycin strong inhibition Bos taurus
0.0004
-
 N-decyl-1-deoxynojirimycin strong inhibition Bos taurus
0.017
-
 N-methyl-1-deoxymannojirimycin very slight inhibition Bos taurus
0.07
-
 N-decanoyl-1-deoxynojirimycin very slight inhibition Bos taurus
0.1
-
 N-5-carboxypentyl-1-deoxymannojirimycin very slight inhibition Bos taurus
0.19
-
 1-deoxymannojirimycin very slight inhibition Bos taurus