BRENDA - Enzyme Database

Protein O-glycosylation in Saccharomyces cerevisiae: the protein O-mannosyltransferases Pmt1p and Pmt2p function as heterodimer

Gentzsch, M.; Immervoll, T.; Tanner, W.; FEBS Lett. 377, 128-130 (1995)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
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
Commentary
Organism
GeneOntology No.
Textmining
2.4.1.109
membrane
-
Saccharomyces cerevisiae
16020
-
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
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
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2.4.1.109
dolichyl phosphate D-mannose + protein
Saccharomyces cerevisiae
-
dolichyl phosphate + O-D-mannosylprotein
-
-
-
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
2.4.1.109
Saccharomyces cerevisiae
-
gene PMT1; gene PMT2
-
Purification (Commentary)
EC Number
Commentary
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
Commentary
Organism
Textmining
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
2.4.1.109
additional information
-
-
Saccharomyces cerevisiae
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.4.1.109
dolichyl phosphate D-mannose + Ac-Tyr-Ala-Thr-Ala-Val-NH2
recombinant yeast overproducing PMT1 and PMT2
638336
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Ala-Thr-Ala-Val-NH2
-
638336
Saccharomyces cerevisiae
ir
2.4.1.109
dolichyl phosphate D-mannose + Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
-
638336
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
-
638336
Saccharomyces cerevisiae
ir
2.4.1.109
dolichyl phosphate D-mannose + AcSSSSSNH2
-
638336
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosyl-AcSSSSSNH2
-
638336
Saccharomyces cerevisiae
ir
2.4.1.109
dolichyl phosphate D-mannose + protein
-
638336
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
-
-
-
2.4.1.109
dolichyl phosphate D-mannose + protein
-
638336
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
638336
Saccharomyces cerevisiae
?
2.4.1.109
dolichyl phosphate D-mannose + protein
-
638336
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
638336
Saccharomyces cerevisiae
ir
2.4.1.109
additional information
PMT1 and PMT2 function as a complex
638336
Saccharomyces cerevisiae
?
-
-
-
-
Subunits
EC Number
Subunits
Commentary
Organism
2.4.1.109
?
x * 78000, PMT2, SDS-PAGE; x * 92000, PMT1, SDS-PAGE
Saccharomyces cerevisiae
2.4.1.109
More
PMT1 and PMT2 function as a complex
Saccharomyces cerevisiae
Cloned(Commentary) (protein specific)
EC Number
Commentary
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 (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.4.1.109
membrane
-
Saccharomyces cerevisiae
16020
-
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
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) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2.4.1.109
dolichyl phosphate D-mannose + protein
Saccharomyces cerevisiae
-
dolichyl phosphate + O-D-mannosylprotein
-
-
-
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
2.4.1.109
immunoaffinity chromatography, co-purification of PMT1 and PMT2 as a complex, no immuno-cross reactivity
Saccharomyces cerevisiae
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
2.4.1.109
additional information
-
-
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.4.1.109
dolichyl phosphate D-mannose + Ac-Tyr-Ala-Thr-Ala-Val-NH2
recombinant yeast overproducing PMT1 and PMT2
638336
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Ala-Thr-Ala-Val-NH2
-
638336
Saccharomyces cerevisiae
ir
2.4.1.109
dolichyl phosphate D-mannose + Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
-
638336
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
-
638336
Saccharomyces cerevisiae
ir
2.4.1.109
dolichyl phosphate D-mannose + AcSSSSSNH2
-
638336
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosyl-AcSSSSSNH2
-
638336
Saccharomyces cerevisiae
ir
2.4.1.109
dolichyl phosphate D-mannose + protein
-
638336
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
-
-
-
2.4.1.109
dolichyl phosphate D-mannose + protein
-
638336
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
638336
Saccharomyces cerevisiae
?
2.4.1.109
dolichyl phosphate D-mannose + protein
-
638336
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
638336
Saccharomyces cerevisiae
ir
2.4.1.109
additional information
PMT1 and PMT2 function as a complex
638336
Saccharomyces cerevisiae
?
-
-
-
-
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
2.4.1.109
?
x * 78000, PMT2, SDS-PAGE; x * 92000, PMT1, SDS-PAGE
Saccharomyces cerevisiae
2.4.1.109
More
PMT1 and PMT2 function as a complex
Saccharomyces cerevisiae