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Literature summary extracted from

  • Walther, T.; Baylac, A.; Alkim, C.; Vax, A.; Cordier, H.; Francois, J.M.
    The PGM3 gene encodes the major phosphoribomutase in the yeast Saccharomyces cerevisiae (2012), FEBS Lett., 586, 4114-4118.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
5.4.2.7 D-Glucose 1,6-bisphosphate required Saccharomyces cerevisiae

Cloned(Commentary)

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

KM Value [mM]

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.4.2.2 Mg2+ required Saccharomyces cerevisiae
5.4.2.7 Mg2+ required Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

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 ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
5.4.2.2 Saccharomyces cerevisiae
-
-
-
5.4.2.7 Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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 ?
-
?

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

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

General Information

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