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Literature summary extracted from

  • Gentzsch, M.; Immervoll, T.; Tanner, W.
    Protein O-glycosylation in Saccharomyces cerevisiae: the protein O-mannosyltransferases Pmt1p and Pmt2p function as heterodimer (1995), FEBS Lett., 377, 128-130.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.109 cloning and overexpression of PMT2 in yeast strain GFUII-4B, showing no alteration of enzyme activity, and co-overexpression with PMT1 in yeast strain TF1.8, leading to 3fold increase in enzyme activity in vitro, thus PMT1 and 2 function as a complex Saccharomyces cerevisiae

Localization

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.4.1.109 78000
-
x * 78000, PMT2, SDS-PAGE Saccharomyces cerevisiae
2.4.1.109 92000
-
x * 92000, PMT1, SDS-PAGE Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.109 dolichyl phosphate D-mannose + protein Saccharomyces cerevisiae
-
dolichyl phosphate + O-D-mannosylprotein
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.109 Saccharomyces cerevisiae
-
gene PMT1
-
2.4.1.109 Saccharomyces cerevisiae
-
gene PMT2
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.109 immunoaffinity chromatography, co-purification of PMT1 and PMT2 as a complex, no immuno-cross reactivity Saccharomyces cerevisiae

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.1.109 additional information
-
-
Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.109 dolichyl phosphate D-mannose + Ac-Tyr-Ala-Thr-Ala-Val-NH2 recombinant yeast overproducing PMT1 and PMT2 Saccharomyces cerevisiae dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Ala-Thr-Ala-Val-NH2
-
ir
2.4.1.109 dolichyl phosphate D-mannose + Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
-
Saccharomyces cerevisiae dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
-
ir
2.4.1.109 dolichyl phosphate D-mannose + AcSSSSSNH2
-
Saccharomyces cerevisiae dolichyl phosphate + O-D-mannosyl-AcSSSSSNH2
-
ir
2.4.1.109 dolichyl phosphate D-mannose + protein
-
Saccharomyces cerevisiae dolichyl phosphate + O-D-mannosylprotein
-
?
2.4.1.109 dolichyl phosphate D-mannose + protein
-
Saccharomyces cerevisiae dolichyl phosphate + O-D-mannosylprotein
-
ir
2.4.1.109 additional information PMT1 and PMT2 function as a complex Saccharomyces cerevisiae ?
-
?

Subunits

EC Number Subunits Comment Organism
2.4.1.109 ? x * 78000, PMT2, SDS-PAGE Saccharomyces cerevisiae
2.4.1.109 ? x * 92000, PMT1, SDS-PAGE Saccharomyces cerevisiae
2.4.1.109 More PMT1 and PMT2 function as a complex Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
2.4.1.109 PMT
-
Saccharomyces cerevisiae
2.4.1.109 protein O-mannosyltransferase
-
Saccharomyces cerevisiae