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Literature summary extracted from

  • Romero, P.A.; Herscovics, A.
    Glycoprotein biosynthesis in Saccharomyces cerevisiae. Characterization of alpha-1,6-mannosyltransferase which initiates outer chain formation (1989), J. Biol. Chem., 264, 1946-1950.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.4.1.232 Triton X-100 requirement, maximum activity at 0.5-2% Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.232 0.35
-
 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)GlcNAc
-
 Saccharomyces cerevisiae
2.4.1.232 0.39
-
 Manalpha(1-2)Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAc
-
 Saccharomyces cerevisiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.1.232 Mn2+ absolute requirement, optimum concentration: 10 mM, Ca2+, Mg2+, Co2+ or Zn2+ cannot substitute for Mn2+ Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.232 additional information Saccharomyces cerevisiae involved in glycoprotein biosynthesis, enzyme catalyzes the first step specific to N-linked oligosaccharide synthesis and the biosynthesis of the outer chain of mannoproteins ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.232 Saccharomyces cerevisiae
-
 mnn1 mutant lacking alpha-1,3-mannosyltransferase
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.232 GDP-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)GlcNAc Man9GlcNAc from rat liver glycoproteins and thyroglobulin, enzyme initiates outer chain synthesis, the mannose residue added is alpha-1,6-linked to the alpha-1,6-mannose residue of the substrate, removal of the alpha-1,2-linked mannose residue from Man9GlcNAc is not essential for enzyme activity Saccharomyces cerevisiae GDP + Manalpha(1-2)[Manalpha(1-6)]Manalpha(1-6)[Manalpha(1-2)Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAc Man10GlcNAc ?
2.4.1.232 GDP-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)GlcNAc Man8GlcNAc from rat liver glycoproteins and thyroglobulin, enzyme initiates outer chain synthesis, the mannose residue added is alpha-1,6-linked to the alpha-1,6-mannose residue of the substrate Saccharomyces cerevisiae GDP + Manalpha(1-2)[Manalpha(1-6)]Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAc Man9GlcNAc ?
2.4.1.232 additional information involved in glycoprotein biosynthesis, enzyme catalyzes the first step specific to N-linked oligosaccharide synthesis and the biosynthesis of the outer chain of mannoproteins Saccharomyces cerevisiae ?
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.232 30
-
 assay at Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.232 7.1 7.6 in Tris maleate buffer Saccharomyces cerevisiae