EC Number | Cloned (Comment) | Organism |
---|---|---|
2.4.1.109 | cloning and overexpression of PMT2 in yeast strain GFUII-4B, showing no alteration of enzyme activity, and co-overexpression with PMT1 in yeast strain TF1.8, leading to 3fold increase in enzyme activity in vitro, thus PMT1 and 2 function as a complex | Saccharomyces cerevisiae |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
2.4.1.109 | membrane | - |
Saccharomyces cerevisiae | 16020 | - |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.4.1.109 | 78000 | - |
x * 78000, PMT2, SDS-PAGE | Saccharomyces cerevisiae |
2.4.1.109 | 92000 | - |
x * 92000, PMT1, SDS-PAGE | Saccharomyces cerevisiae |
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 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.4.1.109 | Saccharomyces cerevisiae | - |
gene PMT1 | - |
2.4.1.109 | Saccharomyces cerevisiae | - |
gene PMT2 | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.4.1.109 | immunoaffinity chromatography, co-purification of PMT1 and PMT2 as a complex, no immuno-cross reactivity | Saccharomyces cerevisiae |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
2.4.1.109 | additional information | - |
- |
Saccharomyces cerevisiae |
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 | recombinant yeast overproducing PMT1 and PMT2 | Saccharomyces cerevisiae | dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Ala-Thr-Ala-Val-NH2 | - |
ir | |
2.4.1.109 | dolichyl phosphate D-mannose + Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2 | - |
Saccharomyces cerevisiae | dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2 | - |
ir | |
2.4.1.109 | dolichyl phosphate D-mannose + AcSSSSSNH2 | - |
Saccharomyces cerevisiae | dolichyl phosphate + O-D-mannosyl-AcSSSSSNH2 | - |
ir | |
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 | - |
Saccharomyces cerevisiae | dolichyl phosphate + O-D-mannosylprotein | - |
ir | |
2.4.1.109 | additional information | PMT1 and PMT2 function as a complex | Saccharomyces cerevisiae | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.4.1.109 | ? | x * 78000, PMT2, SDS-PAGE | Saccharomyces cerevisiae |
2.4.1.109 | ? | x * 92000, PMT1, SDS-PAGE | Saccharomyces cerevisiae |
2.4.1.109 | More | PMT1 and PMT2 function as a complex | Saccharomyces cerevisiae |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.4.1.109 | PMT | - |
Saccharomyces cerevisiae |
2.4.1.109 | protein O-mannosyltransferase | - |
Saccharomyces cerevisiae |