BRENDA - Enzyme Database

Protein O-glycosylation in yeast. The PMT2 gene specifies a second protein O-mannosyltransferase that functions in addition to the PMT-1 encoded activity

Lussier, M.; Gentzsch, M.; Sdicu, A.M.; Bussey, H.; Tanner, W.; J. Biol. Chem. 270, 2770-2775 (1995)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
2.4.1.109
chromosome mapping of PMT1; DNA sequence determination, chromosome mapping
Saccharomyces cerevisiae
Engineering
EC Number
Amino acid exchange
Commentary
Organism
2.4.1.109
additional information
PMT1 and PMT2 double disruption mutant shows severe growth defect but retain residual activity due to an additional enzyme; PMT1 and PMT2 double disruption mutant shows severe growth defect but retain residual activity due to an additional enzyme; PMT2 disruption mutant shows reduced in vitro and in vivo activity; PMT2 haploid mutants grow slightly slower than the wild-type, the enzyme is required but not essential for normal vegetative growth of the cells
Saccharomyces cerevisiae
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.4.1.109
membrane
integral, multiple transmembranal domains; integral, multiple transmembranal domains
Saccharomyces cerevisiae
16020
-
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
2.4.1.109
Mg2+
-
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
P31382
PMT2
-
2.4.1.109
Saccharomyces cerevisiae
-
enzyme form other than PMT2; gene PMT1
-
Posttranslational Modification
EC Number
Posttranslational Modification
Commentary
Organism
2.4.1.109
glycoprotein
PMT1 and PMT2 contain both 3 putative N-glycosylation sites; PMT1 and PMT2 contain both 3 putative N-glycosylation sites
Saccharomyces cerevisiae
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/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-Asn-Pro-Thr-Ser-Val-NH2
-
638338
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
-
638338
Saccharomyces cerevisiae
?
2.4.1.109
dolichyl phosphate D-mannose + protein
-
638338
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
-
-
-
2.4.1.109
dolichyl phosphate D-mannose + protein
-
638338
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
638338
Saccharomyces cerevisiae
?
2.4.1.109
dolichyl phosphate D-mannose + protein
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
638338
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
638338
Saccharomyces cerevisiae
?
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
2.4.1.109
chromosome mapping of PMT1
Saccharomyces cerevisiae
2.4.1.109
DNA sequence determination, chromosome mapping
Saccharomyces cerevisiae
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
2.4.1.109
additional information
PMT1 and PMT2 double disruption mutant shows severe growth defect but retain residual activity due to an additional enzyme
Saccharomyces cerevisiae
2.4.1.109
additional information
PMT1 and PMT2 double disruption mutant shows severe growth defect but retain residual activity due to an additional enzyme; PMT2 disruption mutant shows reduced in vitro and in vivo activity; PMT2 haploid mutants grow slightly slower than the wild-type, the enzyme is required but not essential for normal vegetative growth of the cells
Saccharomyces cerevisiae
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.4.1.109
membrane
integral, multiple transmembranal domains
Saccharomyces cerevisiae
16020
-
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
2.4.1.109
Mg2+
-
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
-
-
-
Posttranslational Modification (protein specific)
EC Number
Posttranslational Modification
Commentary
Organism
2.4.1.109
glycoprotein
PMT1 and PMT2 contain both 3 putative N-glycosylation sites
Saccharomyces cerevisiae
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/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-Asn-Pro-Thr-Ser-Val-NH2
-
638338
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
-
638338
Saccharomyces cerevisiae
?
2.4.1.109
dolichyl phosphate D-mannose + protein
-
638338
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
-
-
-
2.4.1.109
dolichyl phosphate D-mannose + protein
-
638338
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
638338
Saccharomyces cerevisiae
?
2.4.1.109
dolichyl phosphate D-mannose + protein
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
638338
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
638338
Saccharomyces cerevisiae
?