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Literature summary extracted from

  • Gentzsch, M.; Strahl-Bolsinger, S.; Tanner, W.
    A new Dol-P-Man:protein O-D-mannosyltransferase activity from Saccharomyces cerevisiae (1995), Glycobiology, 5, 77-82.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment 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 Comment Organism Structure
2.4.1.109 Mg2+
-
 Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment 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 Comment Organism GeneOntology No. Textmining
2.4.1.109 membrane
-
 Saccharomyces cerevisiae 16020
-

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
-
 enzyme form other than PMT1
-

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
-
 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 Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 Saccharomyces cerevisiae dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Ala-Thr-Ala-Val-NH2
-
 ?
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 the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues Saccharomyces cerevisiae dolichyl phosphate + O-D-mannosylprotein
-
 ?
2.4.1.109 dolichyl phosphate D-mannose + RSPSPSTQ
-
 Saccharomyces cerevisiae dolichyl phosphate + O-D-mannosyl-RSPSPSTQ
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.109 PMT
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment 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 Comment 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