BRENDA - Enzyme Database show
show all sequences of 5.4.2.7

The PGM3 gene encodes the major phosphoribomutase in the yeast Saccharomyces cerevisiae

Walther, T.; Baylac, A.; Alkim, C.; Vax, A.; Cordier, H.; Francois, J.M.; FEBS Lett. 586, 4114-4118 (2012)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
D-Glucose 1,6-bisphosphate
required
Saccharomyces cerevisiae
Cloned(Commentary)
Commentary
Organism
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]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.5
3
alpha-D-ribose 1-phosphate
recombinant His-tagged Pgm2, pH 7.5, 30C
Saccharomyces cerevisiae
0.75
-
alpha-D-ribose 1-phosphate
recombinant His-tagged Pgm3, pH 7.5, 30C
Saccharomyces cerevisiae
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
alpha-D-ribose 1-phosphate
Saccharomyces cerevisiae
-
alpha-D-ribose 5-phosphate
-
-
?
additional information
Saccharomyces cerevisiae
Pgm3 functions as the major phosphoribomutase in vivo
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharomyces cerevisiae
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged Pgm1, Pgm2, and Pgm3 from Escherichia coli strain BL21 (DE3)
Saccharomyces cerevisiae
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.06
-
purified recombinant His-tagged Pgm1, pH 7.5, 30C
Saccharomyces cerevisiae
0.29
-
purified recombinant His-tagged Pgm3, pH 7.5, 30C
Saccharomyces cerevisiae
0.32
-
purified recombinant His-tagged Pgm2, pH 7.5, 30C
Saccharomyces cerevisiae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
alpha-D-ribose 1-phosphate
-
727521
Saccharomyces cerevisiae
alpha-D-ribose 5-phosphate
-
-
-
?
additional information
Pgm3 functions as the major phosphoribomutase in vivo
727521
Saccharomyces cerevisiae
?
-
-
-
-
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
727521
Saccharomyces cerevisiae
?
-
-
-
-
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Saccharomyces cerevisiae
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Saccharomyces cerevisiae
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
D-Glucose 1,6-bisphosphate
required
Saccharomyces cerevisiae
Cloned(Commentary) (protein specific)
Commentary
Organism
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] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.5
3
alpha-D-ribose 1-phosphate
recombinant His-tagged Pgm2, pH 7.5, 30C
Saccharomyces cerevisiae
0.75
-
alpha-D-ribose 1-phosphate
recombinant His-tagged Pgm3, pH 7.5, 30C
Saccharomyces cerevisiae
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
alpha-D-ribose 1-phosphate
Saccharomyces cerevisiae
-
alpha-D-ribose 5-phosphate
-
-
?
additional information
Saccharomyces cerevisiae
Pgm3 functions as the major phosphoribomutase in vivo
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged Pgm1, Pgm2, and Pgm3 from Escherichia coli strain BL21 (DE3)
Saccharomyces cerevisiae
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.06
-
purified recombinant His-tagged Pgm1, pH 7.5, 30C
Saccharomyces cerevisiae
0.29
-
purified recombinant His-tagged Pgm3, pH 7.5, 30C
Saccharomyces cerevisiae
0.32
-
purified recombinant His-tagged Pgm2, pH 7.5, 30C
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
alpha-D-ribose 1-phosphate
-
727521
Saccharomyces cerevisiae
alpha-D-ribose 5-phosphate
-
-
-
?
additional information
Pgm3 functions as the major phosphoribomutase in vivo
727521
Saccharomyces cerevisiae
?
-
-
-
-
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
727521
Saccharomyces cerevisiae
?
-
-
-
-
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Saccharomyces cerevisiae
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Saccharomyces cerevisiae
General Information
General Information
Commentary
Organism
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
General Information (protein specific)
General Information
Commentary
Organism
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
Other publictions for EC 5.4.2.7
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
748749
Meyer
Methanol-essential growth of ...
Escherichia coli, Escherichia coli MeSV1
Nat. Commun.
9
1508
2018
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748271
Rivero
Biosynthesis of an antiviral ...
Escherichia coli, Escherichia coli ATCC 4157
J. Biotechnol.
249
34-41
2017
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6
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746733
Moustafa
A simple assay for determinin ...
Thermotoga maritima
Anal. Biochem.
501
75-81
2016
3
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1
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2
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2
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2
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2
1
1
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2
2
726977
Iverson
Molecular differences between ...
Bacillus cereus, Bacillus cereus DSM 31
Biochemistry
51
1964-1975
2012
1
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1
1
4
1
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1
1
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1
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1
1
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727521
Walther
The PGM3 gene encodes the majo ...
Saccharomyces cerevisiae
FEBS Lett.
586
4114-4118
2012
1
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1
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2
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1
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2
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2
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1
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1
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1
1
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715660
Panosian
Bacillus cereus phosphopentomu ...
Bacillus cereus, Bacillus cereus ATCC 14579
J. Biol. Chem.
286
8043-8054
2011
1
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1
1
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713648
Panosian
Crystallization and preliminar ...
Bacillus cereus, Bacillus cereus ATCC 14579D
Acta Crystallogr. Sect. F
66
811-814
2010
-
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1
1
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4
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705839
Horinouchi
Screening and characterization ...
Escherichia coli, Lysinibacillus sphaericus, Lysinibacillus sphaericus AKU 229
N. Biotechnol.
26
75-82
2009
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1
2
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6
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695174
Taverna-Porro
-
Chemoenzymic preparation of nu ...
Escherichia coli
Tetrahedron Lett.
49
2642-2645
2008
1
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662012
Rashid
Presence of a novel phosphopen ...
Thermococcus kodakarensis
J. Bacteriol.
186
4185-4191
2004
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3348
Hamamoto
Phosphopentomutase of Bacillus ...
Escherichia coli, Geobacillus stearothermophilus, Geobacillus stearothermophilus TH6-2
Biosci. Biotechnol. Biochem.
62
1103-1108
1998
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5
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Barbas
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Escherichia coli
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19
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1991
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3345
Ipata
Induction of phosphoribomutase ...
Bacillus cereus
Biochim. Biophys. Acta
755
253-256
1983
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3346
Barsky
Purification and characterizat ...
Rattus norvegicus
Biochim. Biophys. Acta
743
162-171
1983
2
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3344
Tozzi
A coupled optical enzyme assay ...
Escherichia coli
Anal. Biochem.
123
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3343
Leer
Multiple forms of phosphodeoxy ...
Escherichia coli
Biochemistry
14
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1975
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3342
Nygaard
Nucleoside-catabolizing enzyme ...
Salmonella enterica subsp. enterica serovar Typhimurium
Eur. J. Biochem.
36
267-272
1973
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3341
Munch-Petersen
Mutants constitutive for nucle ...
Escherichia coli
Eur. J. Biochem.
27
208-215
1972
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1
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3340
Hammer-Jespersen
Phosphodeoxyribomutase from Es ...
Escherichia coli
Eur. J. Biochem.
17
397-407
1970
3
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7
2
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3
2
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2
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1
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1
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2
1
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1
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3
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7
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2
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3
2
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1
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1
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2
1
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1
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3339
Kammen
Phosphopentomutases. I. Identi ...
Oryctolagus cuniculus
J. Biol. Chem.
244
4888-4893
1969
2
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1
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1
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1
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2
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1
1
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1
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1
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1
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