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Literature summary for 2.4.1.109 extracted from

  • Strahl-Bolsinger, S.; Tanner, W.
    Protein O-glycosylation in Saccharomyces cerevisiae. Purification and characterization of the dolichyl-phosphate-D-mannose-protein O-D-mannosyltransferase (1991), Eur. J. Biochem., 196, 185-190.
    View publication on PubMed
Search for more literature for 2.4.1.109

Inhibitors

Inhibitors Comment Organism Structure
additional information no inhibition by EDTA Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.4
-
 dolichyl phosphate D-mannose
-
 Saccharomyces cerevisiae
3.3
-
 Tyr-Asn-Pro-Thr-Ser-Val
-
 Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
 Saccharomyces cerevisiae 5783
-
membrane
-
 Saccharomyces cerevisiae 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ 2fold activation Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
92000
-
 x * 92000, SDS-PAGE Saccharomyces cerevisiae
92000
-
 x * 92000, PMT1, SDS-PAGE Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dolichyl phosphate D-mannose + protein Saccharomyces cerevisiae production of cell-wall mannoproteins dolichyl phosphate + O-D-mannosylprotein
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein may contain 4 carbohydrate chains Saccharomyces cerevisiae

Purification (Commentary)

Purification (Comment) Organism
partial Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Saccharomyces cerevisiae
0.0000677
-
 partially purified enzyme Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dolichyl phosphate D-mannose + Lys-Pro-Ser-Gly-Tyr
-
 Saccharomyces cerevisiae dolichyl phosphate + O-D-mannosyl-Lys-Pro-Ser-Gly-Tyr
-
 ?
dolichyl phosphate D-mannose + Lys-Pro-Thr-Gly-Tyr
-
 Saccharomyces cerevisiae dolichyl phosphate + O-D-mannosyl-Lys-Pro-Thr-Gly-Tyr
-
 ?
dolichyl phosphate D-mannose + Lys-Pro-Thr-Pro-Tyr
-
 Saccharomyces cerevisiae dolichyl phosphate + O-D-mannosyl-Lys-Pro-Thr-Pro-Tyr
-
 ?
dolichyl phosphate D-mannose + Pro-Thr-Val
-
 Saccharomyces cerevisiae dolichyl phosphate + O-D-mannosyl-Pro-Thr-Val
-
 ?
dolichyl phosphate D-mannose + Pro-Tyr-Thr-Val
-
 Saccharomyces cerevisiae dolichyl phosphate + O-D-mannosyl-Pro-Tyr-Thr-Val
-
 ?
dolichyl phosphate D-mannose + protein
-
 Saccharomyces cerevisiae dolichyl phosphate + O-D-mannosylprotein
-
 ?
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
-
 ?
dolichyl phosphate D-mannose + protein acidic amino acids strongly inhibit acceptor activity, as do glycine and proline residues as amino-terminal and carboxy-terminal neighbours Saccharomyces cerevisiae dolichyl phosphate + O-D-mannosylprotein
-
 ?
dolichyl phosphate D-mannose + protein production of cell-wall mannoproteins Saccharomyces cerevisiae dolichyl phosphate + O-D-mannosylprotein
-
 ?
dolichyl phosphate D-mannose + Tyr-Asn-Leu-Thr-Ser-Val
-
 Saccharomyces cerevisiae dolichyl phosphate + O-D-mannosyl-Tyr-Asn-Leu-Thr-Ser-Val
-
 ?
dolichyl phosphate D-mannose + Tyr-Asn-Pro-Thr-Ser-Val
-
 Saccharomyces cerevisiae dolichyl phosphate + O-D-mannosyl-Tyr-Asn-Pro-Thr-Ser-Val
-
 ?

Subunits

Subunits Comment Organism
? x * 92000, SDS-PAGE Saccharomyces cerevisiae
? x * 92000, PMT1, SDS-PAGE Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Saccharomyces cerevisiae