EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
5.4.2.7 | D-Glucose 1,6-bisphosphate | required | Saccharomyces cerevisiae |
EC Number | Cloned (Comment) | Organism |
---|---|---|
5.4.2.2 | genes pgm1, pgm2, and pgm3, cloning in Escherichia coli strain DH5alpha, expression of His-tagged enzymes in Escherichia coli strain BL21 (DE3) | Saccharomyces cerevisiae |
5.4.2.7 | genes pgm1, pgm2, and pgm3, cloning in Escherichia coli strain DH5alpha, expression of His-tagged enzymes in Escherichia coli strain BL21 (DE3) | Saccharomyces cerevisiae |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
5.4.2.2 | 0.026 | - |
alpha-D-glucose 1-phosphate | recombinant His-tagged Pgm2, pH 7.5, 30°C | Saccharomyces cerevisiae | |
5.4.2.2 | 0.06 | - |
alpha-D-glucose 1-phosphate | recombinant His-tagged Pgm1, pH 7.5, 30°C | Saccharomyces cerevisiae | |
5.4.2.2 | 0.112 | - |
alpha-D-glucose 1-phosphate | recombinant His-tagged Pgm3, pH 7.5, 30°C | Saccharomyces cerevisiae | |
5.4.2.7 | 0.5 | 3 | alpha-D-ribose 1-phosphate | recombinant His-tagged Pgm2, pH 7.5, 30°C | Saccharomyces cerevisiae | |
5.4.2.7 | 0.75 | - |
alpha-D-ribose 1-phosphate | recombinant His-tagged Pgm3, pH 7.5, 30°C | Saccharomyces cerevisiae |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
5.4.2.2 | Mg2+ | required | Saccharomyces cerevisiae | |
5.4.2.7 | Mg2+ | required | Saccharomyces cerevisiae |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.4.2.2 | alpha-D-glucose 1-phosphate | Saccharomyces cerevisiae | - |
alpha-D-glucose 6-phosphate | - |
? | |
5.4.2.2 | additional information | Saccharomyces cerevisiae | Pgm3 functions as the major phosphoribomutase in vivo | ? | - |
? | |
5.4.2.7 | alpha-D-ribose 1-phosphate | Saccharomyces cerevisiae | - |
alpha-D-ribose 5-phosphate | - |
? | |
5.4.2.7 | additional information | Saccharomyces cerevisiae | Pgm3 functions as the major phosphoribomutase in vivo | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
5.4.2.2 | Saccharomyces cerevisiae | - |
- |
- |
5.4.2.7 | Saccharomyces cerevisiae | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
5.4.2.2 | recombinant His-tagged Pgm1, Pgm2, and Pgm3 from Escherichia coli strain BL21 (DE3) | Saccharomyces cerevisiae |
5.4.2.7 | recombinant His-tagged Pgm1, Pgm2, and Pgm3 from Escherichia coli strain BL21 (DE3) | Saccharomyces cerevisiae |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
5.4.2.2 | 0.1 | 1 | purified recombinant His-tagged Pgm3, pH 7.5, 30°C | Saccharomyces cerevisiae |
5.4.2.2 | 0.24 | - |
purified recombinant His-tagged Pgm1, pH 7.5, 30°C | Saccharomyces cerevisiae |
5.4.2.2 | 33.7 | - |
purified recombinant His-tagged Pgm2, pH 7.5, 30°C | Saccharomyces cerevisiae |
5.4.2.7 | 0.06 | - |
purified recombinant His-tagged Pgm1, pH 7.5, 30°C | Saccharomyces cerevisiae |
5.4.2.7 | 0.29 | - |
purified recombinant His-tagged Pgm3, pH 7.5, 30°C | Saccharomyces cerevisiae |
5.4.2.7 | 0.32 | - |
purified recombinant His-tagged Pgm2, pH 7.5, 30°C | Saccharomyces cerevisiae |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.4.2.2 | alpha-D-glucose 1-phosphate | - |
Saccharomyces cerevisiae | alpha-D-glucose 6-phosphate | - |
? | |
5.4.2.2 | additional information | Pgm3 functions as the major phosphoribomutase in vivo | Saccharomyces cerevisiae | ? | - |
? | |
5.4.2.2 | additional information | phosphoglucomutases Pgm1, Pgm2, and Pgm3, EC 5.4.2.2, of Saccharomyces cerevisiae show ability to interconvert ribose-1-phosphate and ribose-5-phosphate. The purified proteins, studied in vitro with regard to their kinetic properties on glucose-1-phosphate and ribose-1-phosphate, are all active on both substrates with Pgm1 exhibiting only residual activity on ribose-1-phosphate. The Pgm2 and Pgm3 proteins have almost equal kinetic properties on ribose-1-phosphate, but Pgm2 has a 2000times higher preference for glucose-1-phosphate when compared to Pgm3 | Saccharomyces cerevisiae | ? | - |
? | |
5.4.2.7 | alpha-D-ribose 1-phosphate | - |
Saccharomyces cerevisiae | alpha-D-ribose 5-phosphate | - |
? | |
5.4.2.7 | additional information | Pgm3 functions as the major phosphoribomutase in vivo | Saccharomyces cerevisiae | ? | - |
? | |
5.4.2.7 | additional information | phosphoglucomutases Pgm1, Pgm2, and Pgm3, EC 5.4.2.2, of Saccharomyces cerevisiae show ability to interconvert ribose-1-phosphate and ribose-5-phosphate. The purified proteins, studied in vitro with regard to their kinetic properties on glucose-1-phosphate and ribose-1-phosphate, are all active on both substrates with Pgm1 exhibiting only residual activity on ribose-1-phosphate. The Pgm2 and Pgm3 proteins have almost equal kinetic properties on ribose-1-phosphate, but Pgm2 has a 2000times higher preference for glucose-1-phosphate when compared to Pgm3 | Saccharomyces cerevisiae | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
5.4.2.2 | PGM | - |
Saccharomyces cerevisiae |
5.4.2.2 | PGM1 | - |
Saccharomyces cerevisiae |
5.4.2.2 | PGM2 | - |
Saccharomyces cerevisiae |
5.4.2.2 | PGM3 | - |
Saccharomyces cerevisiae |
5.4.2.7 | PGM3 | - |
Saccharomyces cerevisiae |
5.4.2.7 | Phosphoribomutase | - |
Saccharomyces cerevisiae |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
5.4.2.2 | 30 | - |
assay at | Saccharomyces cerevisiae |
5.4.2.7 | 30 | - |
assay at | Saccharomyces cerevisiae |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
5.4.2.2 | 7.5 | - |
assay at | Saccharomyces cerevisiae |
5.4.2.7 | 7.5 | - |
assay at | Saccharomyces cerevisiae |
EC Number | General Information | Comment | Organism |
---|---|---|---|
5.4.2.2 | malfunction | only mutants with a deletion of PGM3, not of PGM1 or PGM2, hyperaccumulate ribose-1-phosphate | Saccharomyces cerevisiae |
5.4.2.7 | malfunction | only a deletion mutant of PGM3, not of PGM1 or PGM2, hyperaccumulates ribose-1-phosphate, and shows a strongly increased concentration of ribose 1-phosphate and completely defective recycling of ribose 1-phosphate upon glucose-induced purine nucleoside recycling via the purine salvage pathway | Saccharomyces cerevisiae |