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Literature summary for 3.2.1.209 extracted from

  • Jelinek-Kelly, S.; Herscovics, A.
    Glycoprotein biosynthesis in Saccharomyces cerevisiae. Purification of the alpha-mannosidase which removes one specific mannose residue from Man9GlcNAc (1988), J. Biol. Chem., 263, 14757-14763.
    View publication on PubMed
Search for more literature for 3.2.1.209

Inhibitors

Inhibitors Comment Organism Structure
Co2+
-
 Saccharomyces cerevisiae
EDTA addition of Ca2+ reverses inhibitory effect Saccharomyces cerevisiae
Mg2+
-
 Saccharomyces cerevisiae
Mn2+
-
 Saccharomyces cerevisiae
Zn2+
-
 Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Saccharomyces cerevisiae 16020
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
75000
-
 gel filtration Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Man9GlcNAc + H2O Saccharomyces cerevisiae highly specific soluble catalytic domain of a larger membrane-bound form, does not act on synthetic substrates Man8GlcNAc + alpha-D-mannopyranose releases only one specific mannopyranose residue ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
to homogeneity, chromatography steps Saccharomyces cerevisiae

Source Tissue

Source Tissue Comment Organism Textmining
cell culture catalytically active soluble domain, released from endogenous proteases Saccharomyces cerevisiae
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Man9GlcNAc + H2O highly specific soluble catalytic domain of a larger membrane-bound form, does not act on synthetic substrates Saccharomyces cerevisiae Man8GlcNAc + alpha-D-mannopyranose releases only one specific mannopyranose residue ?