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Literature summary for 2.4.1.109 extracted from
- A new Dol-P-Man:protein O-D-mannosyltransferase activity from Saccharomyces cerevisiae (1995), Glycobiology, 5, 77-82.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| 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
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | - |
Saccharomyces cerevisiae |  |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 2 | - |
Ac-Tyr-Ala-Thr-Ala-Val-NH2 | PMT1 | Saccharomyces cerevisiae | |
| 10 | - |
RSPSPSTQ | additional enzyme form | Saccharomyces cerevisiae | |
| 15 | - |
Ac-Tyr-Ala-Thr-Ala-Val-NH2 | additional enzyme form | Saccharomyces cerevisiae | |
| 20 | - |
RSPSPSTQ | PMT1 | Saccharomyces cerevisiae | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | - |
Saccharomyces cerevisiae | 16020 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| dolichyl phosphate D-mannose + protein | Saccharomyces cerevisiae | - |
dolichyl phosphate + O-D-mannosylprotein | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
gene PMT1 | - |
| Saccharomyces cerevisiae | - |
enzyme form other than PMT1 | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 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)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | - |
? | |
| 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 + RSPSPSTQ | - |
Saccharomyces cerevisiae | dolichyl phosphate + O-D-mannosyl-RSPSPSTQ | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PMT | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 22 | - |
additional enzyme form | Saccharomyces cerevisiae |
| 30 | - |
PMT1 | Saccharomyces cerevisiae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | - |
PMT1 null mutant, optimum of the additional enzyme form | Saccharomyces cerevisiae |
| 7.5 | - |
PMT1 wild-type | Saccharomyces cerevisiae |
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