BRENDA - Enzyme Database

Mannosylphosphoryldolichol-mediated O-mannosylation of yeast glycoproteins: stereospecificity and recognition of the alpha-isoprene unit by a purified mannosyltransferase

Dotson, S.B.; Rush, J.S.; Ricketts, A.D.; Waechter, C.J.; Arch. Biochem. Biophys. 316, 773-779 (1995)

Data extracted from this reference:

General Stability
EC Number
General Stability
Organism
2.4.1.109
stable in solution with deoxycholate and CHAPS
Saccharomyces cerevisiae
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
2.4.1.109
glycerol
at 20% inhibitory
Saccharomyces cerevisiae
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.4.1.109
membrane
-
Saccharomyces cerevisiae
16020
-
2.4.1.109
microsome
-
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
-
Purification (Commentary)
EC Number
Commentary
Organism
2.4.1.109
partial; solubilization with 0.5% deoxycholate and 1.2% CHAPS
Saccharomyces cerevisiae
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
2.4.1.109
0.0035
-
partially purified enzyme
Saccharomyces cerevisiae
Storage Stability
EC Number
Storage Stability
Organism
2.4.1.109
-80C, partially purified enzyme, indefinitely stable
Saccharomyces cerevisiae
2.4.1.109
23C, partially purified enzyme, 2% glycerol, at least 12 h stable
Saccharomyces cerevisiae
2.4.1.109
4-23C, partially purified enzyme, stable for at least 1 week
Saccharomyces cerevisiae
2.4.1.109
4C, solubilized with 0.5% Triton X-100, loss of 80% activity within 5 days
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 + biotin-Tyr-Ala-Thr-Ala-Val-NH2
-
638334
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosyl-N-biotinyl-Tyr-Ala-Thr-Ala-Val-NH2
-
638334
Saccharomyces cerevisiae
?
2.4.1.109
dolichyl phosphate D-mannose + protein
-
638334
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
-
-
-
2.4.1.109
dolichyl phosphate D-mannose + protein
-
638334
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
638334
Saccharomyces cerevisiae
?
2.4.1.109
dolichyl phosphate D-mannose + protein
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
638334
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
638334
Saccharomyces cerevisiae
?
2.4.1.109
dolichyl phosphate D-mannose + protein
preferred chain lengthin decreasing order: C100, C80, C55, C35
638334
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
638334
Saccharomyces cerevisiae
?
2.4.1.109
dolichyl phosphate D-mannose + protein
strictly stereospecific for the anomeric configuration of phosphoryl-linkage of the donor substrate, a saturated alpha-isoprene unit in the dolichyl moiety is required
638334
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
638334
Saccharomyces cerevisiae
?
2.4.1.109
dolichyl phosphate D-mannose + Tyr-Asn-Pro-Thr-Ser-Val-NH2
-
638334
Saccharomyces cerevisiae
dolichyl phosphate + O-alpha-D-mannosyl-Tyr-Asn-Pro-Thr-Ser-Val-NH2
-
638334
Saccharomyces cerevisiae
?
Temperature Optimum [C]
EC Number
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
2.4.1.109
30
-
assay at
Saccharomyces cerevisiae
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.4.1.109
7
-
assay at
Saccharomyces cerevisiae
pH Stability
EC Number
pH Stability
pH Stability Maximum
Commentary
Organism
2.4.1.109
4.9
-
inactivation below pH 4.9
Saccharomyces cerevisiae
General Stability (protein specific)
EC Number
General Stability
Organism
2.4.1.109
stable in solution with deoxycholate and CHAPS
Saccharomyces cerevisiae
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
2.4.1.109
glycerol
at 20% inhibitory
Saccharomyces cerevisiae
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.4.1.109
membrane
-
Saccharomyces cerevisiae
16020
-
2.4.1.109
microsome
-
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
partial; solubilization with 0.5% deoxycholate and 1.2% CHAPS
Saccharomyces cerevisiae
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
2.4.1.109
0.0035
-
partially purified enzyme
Saccharomyces cerevisiae
Storage Stability (protein specific)
EC Number
Storage Stability
Organism
2.4.1.109
-80C, partially purified enzyme, indefinitely stable
Saccharomyces cerevisiae
2.4.1.109
23C, partially purified enzyme, 2% glycerol, at least 12 h stable
Saccharomyces cerevisiae
2.4.1.109
4-23C, partially purified enzyme, stable for at least 1 week
Saccharomyces cerevisiae
2.4.1.109
4C, solubilized with 0.5% Triton X-100, loss of 80% activity within 5 days
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 + biotin-Tyr-Ala-Thr-Ala-Val-NH2
-
638334
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosyl-N-biotinyl-Tyr-Ala-Thr-Ala-Val-NH2
-
638334
Saccharomyces cerevisiae
?
2.4.1.109
dolichyl phosphate D-mannose + protein
-
638334
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
-
-
-
2.4.1.109
dolichyl phosphate D-mannose + protein
-
638334
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
638334
Saccharomyces cerevisiae
?
2.4.1.109
dolichyl phosphate D-mannose + protein
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
638334
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
638334
Saccharomyces cerevisiae
?
2.4.1.109
dolichyl phosphate D-mannose + protein
preferred chain lengthin decreasing order: C100, C80, C55, C35
638334
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
638334
Saccharomyces cerevisiae
?
2.4.1.109
dolichyl phosphate D-mannose + protein
strictly stereospecific for the anomeric configuration of phosphoryl-linkage of the donor substrate, a saturated alpha-isoprene unit in the dolichyl moiety is required
638334
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
638334
Saccharomyces cerevisiae
?
2.4.1.109
dolichyl phosphate D-mannose + Tyr-Asn-Pro-Thr-Ser-Val-NH2
-
638334
Saccharomyces cerevisiae
dolichyl phosphate + O-alpha-D-mannosyl-Tyr-Asn-Pro-Thr-Ser-Val-NH2
-
638334
Saccharomyces cerevisiae
?
Temperature Optimum [C] (protein specific)
EC Number
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
2.4.1.109
30
-
assay at
Saccharomyces cerevisiae
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.4.1.109
7
-
assay at
Saccharomyces cerevisiae
pH Stability (protein specific)
EC Number
pH Stability
pH Stability Maximum
Commentary
Organism
2.4.1.109
4.9
-
inactivation below pH 4.9
Saccharomyces cerevisiae