BRENDA - Enzyme Database

A new Dol-P-Man:protein O-D-mannosyltransferase activity from Saccharomyces cerevisiae

Gentzsch, M.; Strahl-Bolsinger, S.; Tanner, W.; Glycobiology 5, 77-82 (1995)

Data extracted from this reference:

Engineering
EC Number
Amino acid exchange
Commentary
Organism
2.4.1.109
additional information
PMT1 null mutant shows increased heat lability, alpa-D-mannose transfer only to serine residue of the substrate peptide Ac-YNPTSV-NH2, not to threonine and valine like with the wild-type
Saccharomyces cerevisiae
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
2.4.1.109
Mg2+
-
Saccharomyces cerevisiae
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.4.1.109
2
-
Ac-Tyr-Ala-Thr-Ala-Val-NH2
PMT1
Saccharomyces cerevisiae
2.4.1.109
10
-
RSPSPSTQ
additional enzyme form
Saccharomyces cerevisiae
2.4.1.109
15
-
Ac-Tyr-Ala-Thr-Ala-Val-NH2
additional enzyme form
Saccharomyces cerevisiae
2.4.1.109
20
-
RSPSPSTQ
PMT1
Saccharomyces cerevisiae
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.4.1.109
membrane
-
Saccharomyces cerevisiae
16020
-
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
-
enzyme form other than PMT1; gene PMT1
-
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
-
specific activity of the additional enzyme form is 7fold higher than that of PMT1, substrate Ac-YNPTSV-NH2
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
PMT1 transfers preferably to the threonine and valine residues, the additional enzyme form prefers the serine residue, both depending on the sequence of the acceptor substrate peptide
638337
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Ala-Thr-Ala-Val-NH2
-
638337
Saccharomyces cerevisiae
?
2.4.1.109
dolichyl phosphate D-mannose + protein
-
638337
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
-
-
-
2.4.1.109
dolichyl phosphate D-mannose + protein
-
638337
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
638337
Saccharomyces cerevisiae
?
2.4.1.109
dolichyl phosphate D-mannose + protein
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
638337
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
638337
Saccharomyces cerevisiae
?
2.4.1.109
dolichyl phosphate D-mannose + RSPSPSTQ
-
638337
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosyl-RSPSPSTQ
-
638337
Saccharomyces cerevisiae
?
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
2.4.1.109
22
-
additional enzyme form
Saccharomyces cerevisiae
2.4.1.109
30
-
PMT1
Saccharomyces cerevisiae
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.4.1.109
6.5
-
PMT1 null mutant, optimum of the additional enzyme form
Saccharomyces cerevisiae
2.4.1.109
7.5
-
PMT1 wild-type
Saccharomyces cerevisiae
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
2.4.1.109
additional information
PMT1 null mutant shows increased heat lability, alpa-D-mannose transfer only to serine residue of the substrate peptide Ac-YNPTSV-NH2, not to threonine and valine like with the wild-type
Saccharomyces cerevisiae
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
2.4.1.109
Mg2+
-
Saccharomyces cerevisiae
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.4.1.109
2
-
Ac-Tyr-Ala-Thr-Ala-Val-NH2
PMT1
Saccharomyces cerevisiae
2.4.1.109
10
-
RSPSPSTQ
additional enzyme form
Saccharomyces cerevisiae
2.4.1.109
15
-
Ac-Tyr-Ala-Thr-Ala-Val-NH2
additional enzyme form
Saccharomyces cerevisiae
2.4.1.109
20
-
RSPSPSTQ
PMT1
Saccharomyces cerevisiae
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.4.1.109
membrane
-
Saccharomyces cerevisiae
16020
-
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
-
-
-
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
-
specific activity of the additional enzyme form is 7fold higher than that of PMT1, substrate Ac-YNPTSV-NH2
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
PMT1 transfers preferably to the threonine and valine residues, the additional enzyme form prefers the serine residue, both depending on the sequence of the acceptor substrate peptide
638337
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Ala-Thr-Ala-Val-NH2
-
638337
Saccharomyces cerevisiae
?
2.4.1.109
dolichyl phosphate D-mannose + protein
-
638337
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
-
-
-
2.4.1.109
dolichyl phosphate D-mannose + protein
-
638337
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
638337
Saccharomyces cerevisiae
?
2.4.1.109
dolichyl phosphate D-mannose + protein
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
638337
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosylprotein
-
638337
Saccharomyces cerevisiae
?
2.4.1.109
dolichyl phosphate D-mannose + RSPSPSTQ
-
638337
Saccharomyces cerevisiae
dolichyl phosphate + O-D-mannosyl-RSPSPSTQ
-
638337
Saccharomyces cerevisiae
?
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
2.4.1.109
22
-
additional enzyme form
Saccharomyces cerevisiae
2.4.1.109
30
-
PMT1
Saccharomyces cerevisiae
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.4.1.109
6.5
-
PMT1 null mutant, optimum of the additional enzyme form
Saccharomyces cerevisiae
2.4.1.109
7.5
-
PMT1 wild-type
Saccharomyces cerevisiae