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Literature summary extracted from

  • Tempel, W.; Karaveg, K.; Liu, Z.J.; Rose, J.; Wang, B.C.; Moremen, K.W.
    Structure of mouse Golgi alpha-mannosidase IA reveals the molecular basis for substrate specificity among class 1 (family 47 glycosylhydrolase) alpha1,2-mannosidases (2004), J. Biol. Chem., 279, 29774-29786.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.24 expression of Golgi alpha-mannosidase IA in fusion with the yeast alpha-factor signal sequence in Pichia pastoris strain GS115 Mus musculus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.24 30 mg/ml purified recombinant Golgi alpha-mannosidase IA in 20 mM MES, pH 6.5, 150 mM NaCl, 5 mM CaCl2, and 0.75 M NDSB-201, crystallization of free enzyme by microbatch method using a precipitation solution containing 15-20% PEG 4000 at pH 4.5-6.5, cocrystallization of 1-deoxymannojirimycin bound to the enzyme by hanging drop vapour diffusion method at 37°C, 0.001 ml of a solution containing 200 mM 1-deoxymannojirimycin is mixed with an equal volume of crystallization solution containing 100 mM MES and 100 mM Tris-HCl, pH 6.0, and 25-35% PEG 4000, 2 days at 18°C, X-ray diffraction structure determination and analysis at 1.5 A resolution, structure modelling Mus musculus
3.2.1.113 hanging drop vapor diffusion method, 15 A resolution Mus musculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.24 1-deoxymannojirimycin class 1 alpha1,2-mannosidase inhibitor Mus musculus
3.2.1.24 kifunensine class 1 alpha1,2-mannosidase inhibitor Mus musculus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.24 endoplasmic reticulum ER alpha-mannosidase I Mus musculus 5783
-
3.2.1.24 Golgi apparatus Golgi alpha-mannosidase IA Mus musculus 5794
-
3.2.1.113 Golgi apparatus
-
 Mus musculus 5794
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.24 Ca2+ is critical in coordination of the enzyme's (alphaalpha)7 barrel structure, located at the base of the barrel Mus musculus
3.2.1.113 Ca2+ the enzyme assumes an (alphaalpha)7 barrel structure with a Ca2+ ion coordinated at the bas of the barrel Mus musculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.24 Man8GlcNAc2 + 3 H2O Mus musculus Golgi alpha-mannosidase in vivo Man5GlcNAc2 + 3 D-mannose
-
 ?
3.2.1.24 Man9GlcNAc2 + H2O Mus musculus endoplasmic reticulum alpha-mannosidase in vivo Man8GlcNAc2 + mannose
-
 ?
3.2.1.24 additional information Mus musculus class 1 alpha1,2-mannosidases of glycosylhydrolase family 47 play critical roles in the maturation of Asn-linked glycoproteins in the endoplasmic reticulum and Golgi complex as well as in the recognition and timing of disposal of terminally unfolded proteins by ER-associated degradation, overview ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.24 Mus musculus
-
-
-
3.2.1.113 Mus musculus P45700 recombinant
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.24 recombinant yeast alpha-factor signal sequence-fusion enzyme from Pichia pastoris strain GS115 by ion exchange and hydrophobic interaction chromatography, eluent is ammonium sulfate, and gel filtration Mus musculus
3.2.1.113
-
 Mus musculus

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.24 2-O-alpha-D-mannopyranosyl-D-mannopyranose + H2O = 2 alpha-D-mannopyranose active site structure and catalytic residues, e.g. Asn515 involved in substrate binding, reaction mechanism and processing steps, overview Mus musculus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.24 Man6GlcNAc2 + H2O slow reaction of the Golgi alpha-mannosidase in vitro Mus musculus Man5GlcNAc2 + mannose
-
 ?
3.2.1.24 Man8GlcNAc2 + 3 H2O Golgi alpha-mannosidase in vivo Mus musculus Man5GlcNAc2 + 3 D-mannose
-
 ?
3.2.1.24 Man8GlcNAc2 + 3 H2O slow reaction of the endoplasmic reticulum alpha-mannosidase in vitro Mus musculus Man5GlcNAc2 + 3 D-mannose
-
 ?
3.2.1.24 Man9GlcNAc2 + 3 H2O fast reaction of the Golgi alpha-mannosidase in vitro Mus musculus Man6GlcNAc2 + 3 mannose
-
 ?
3.2.1.24 Man9GlcNAc2 + H2O endoplasmic reticulum alpha-mannosidase in vivo Mus musculus Man8GlcNAc2 + mannose
-
 ?
3.2.1.24 Man9GlcNAc2 + H2O fast reaction of the endoplasmic reticulum alpha-mannosidase in vitro Mus musculus Man8GlcNAc2 + mannose
-
 ?
3.2.1.24 additional information class 1 alpha1,2-mannosidases of glycosylhydrolase family 47 play critical roles in the maturation of Asn-linked glycoproteins in the endoplasmic reticulum and Golgi complex as well as in the recognition and timing of disposal of terminally unfolded proteins by ER-associated degradation, overview Mus musculus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.24 More structure analysis, the enzyme has an (alphaalpha)7 barrel structure with a coordinating Ca2+ ion, overview Mus musculus

Synonyms

EC Number Synonyms Comment Organism
3.2.1.24 alpha-mannosidase I
-
 Mus musculus
3.2.1.24 alpha-mannosidase IA
-
 Mus musculus
3.2.1.24 alpha1,2-mannosidase
-
 Mus musculus
3.2.1.24 More the enzyme belongs to the class 1 alpha1,2-mannosidases of glycosylhydrolase family 47 Mus musculus
3.2.1.113 alpha1,2-mannosidase
-
 Mus musculus