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Literature summary for 2.4.1.232 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

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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
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

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
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 ?
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]

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

pH Optimum

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