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Literature summary for 3.2.1.113 extracted from

  • Schweden, J.; Bause, E.
    Characterization of trimming Man9-mannosidase from pig liver. Purification of a catalytically active fragment and evidence for the transmembrane nature of the intact 65 kDa enzyme (1989), Biochem. J., 264, 347-355.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.2.1.113

General Stability

General Stability Organism
native enzyme protein is highly susceptible to proteolytic cleavage, not by glucopeptidase F Sus scrofa

Inhibitors

Inhibitors Comment Organism Structure
1-deoxymannojirimycin
-
 Sus scrofa
Basic sugar analogs of mannose strong Sus scrofa
Cu2+
-
 Sus scrofa
additional information no inhibition by swainsonine; no or little inhibition by N,N-dimethyl-1-deoxymannojirimycin Sus scrofa
N-Methyl-deoxymannojirimycin
-
 Sus scrofa

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Sus scrofa 16020
-
microsome trans-membrane protein with cytosolic domain Sus scrofa
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activation Sus scrofa
Ca2+ most effective cation Sus scrofa
Mg2+ activation Sus scrofa
Mg2+ less effective than Ca2+ Sus scrofa
Zn2+ activation, less effective than Ca2+ Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
49000
-
 1 * 49000, SDS-PAGE Sus scrofa
65000
-
 detected in freshly prepared crude microsomal extracts using polyclonal antibodies, during purification the native enzyme, MW 65000, loses a membrane-spanning domain without losing its catalytic activity Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
affinity chromatography on immobilized N-5-carboxypentyl-1-deoxymannojirimycin Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O removes 3 of the 4 alpha1,2-linked mannosyl residues Sus scrofa (Man)6(GlcNAc)2 + D-mannose
-
 ?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O highly active on alpha(1-2) linked mannooligosaccharides Sus scrofa (Man)6(GlcNAc)2 + D-mannose
-
 ?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
-
 Sus scrofa ? + D-mannose
-
 ?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
-
 Sus scrofa ? + D-mannose
-
 ?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAc + H2O very poor substrate Sus scrofa (Man)5(GlcNAc)2 + D-mannose
-
 ?
additional information no substrate: 4-methylumbelliferyl-alpha-mannoside Sus scrofa ?
-
 ?
additional information pig liver enzyme substrate specificity resembles that of calf liver enzyme Sus scrofa ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 49000, SDS-PAGE Sus scrofa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Sus scrofa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
 Sus scrofa

pH Range

pH Minimum pH Maximum Comment Organism
5.2 6.7 about half-maximal activity at pH 5.2 and 6.7 Sus scrofa