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Information on EC 5.4.2.7 - phosphopentomutase
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EC Tree
5.4.2.7 phosphopentomutaseIUBMB Comments
Also converts 2-deoxy-alpha-D-ribose 1-phosphate into 2-deoxy-D-ribose 5-phosphate. alpha-D-Ribose 1,5-bisphosphate, 2-deoxy-alpha-D-ribose 1,5-bisphosphate, or alpha-D-glucose 1,6-bisphosphate can act as cofactor.
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Word Map
- 5.4.2.7
- nucleoside
- purine
- 5-phosphate
- phosphoglucomutase
- deoxyriboaldolase
- 2-deoxyribose
- ribose-5-phosphate
-
nucleobase
- phosphorylases
- deoxyribonucleosides
- 2'-deoxyribonucleoside
- ribokinase
- 1,6-diphosphate
-
phosphorolysis
-
phosphomutases
- analysis
- biotechnology
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
phosphopentomutase, phosphoribomutase, phosphodeoxyribomutase, deoxyribomutase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-D-Glucose-1,6-bisphosphate:deoxy-D-ribose-1-phosphate phosphotransferase
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-
-
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deoB
Deoxyribomutase
-
-
-
-
Deoxyribose phosphomutase
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-
-
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EC 2.7.5.6
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-
formerly
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Phosphodeoxyribomutase
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-
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Phosphomutase, deoxyribose
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-
-
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phosphopentomutase
Phosphoribomutase
PPM
PPMase
Phosphoribomutase
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-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alpha-D-ribose 1-phosphate = D-ribose 5-phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
group transfer
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-
intramolecular, phosphate group
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isomerization
isomerization
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-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
alpha-D-ribose 1,5-phosphomutase
Also converts 2-deoxy-alpha-D-ribose 1-phosphate into 2-deoxy-D-ribose 5-phosphate. alpha-D-Ribose 1,5-bisphosphate, 2-deoxy-alpha-D-ribose 1,5-bisphosphate, or alpha-D-glucose 1,6-bisphosphate can act as cofactor.
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CAS REGISTRY NUMBER
COMMENTARY
9026-77-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-deoxy-D-ribose 1-phosphate
2-deoxy-D-ribose 5-phosphate
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-
-
?
Glucose 1-phosphate
?
-
at 2.4% of the activity relative to ribose 1-phosphate
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-
?
Ribose 1-phosphate
?
-
inducible enzyme. In order to enter the pentose phosphate cycle ribose 1-phosphate must be isomerized to ribose 5-phosphate
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-
?
2,3-dideoxyribose 5-phosphate
2,3-dideoxyribose 1-phosphate
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-
-
?, r
2,3-dideoxyribose 5-phosphate
2,3-dideoxyribose 1-phosphate
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-
-
?
2-deoxy-D-ribose 5-phosphate
2-deoxy-D-ribose 1-phosphate
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-
-
r
2-deoxyribose 5-phosphate
2-deoxyribose 1-phosphate
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at 156% of the activity relative to ribose 5-phosphate
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?
2-deoxyribose 5-phosphate
2-deoxyribose 1-phosphate
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at 156% of the activity relative to ribose 5-phosphate
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?
alpha-D-ribose 1-phosphate
D-ribose 5-phosphate
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PPM is involve in the salvage pathway of nucleoside synthesis
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?
alpha-D-ribose 1-phosphate
D-ribose 5-phosphate
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-
-
?
D-Arabinose 5-phosphate
D-Arabinose 1-phosphate
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at 8.61% of the activity relative to ribose 5-phosphate
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-
?
D-Arabinose 5-phosphate
D-Arabinose 1-phosphate
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at 8.61% of the activity relative to ribose 5-phosphate
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-
?
D-ribose 1-phosphate
D-ribose 5-phosphate
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only the reverse reaction is mentioned: D-ribose 5-phosphate to D-ribose 1-phosphate
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-
?
D-ribose 1-phosphate
D-ribose 5-phosphate
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only the reverse reaction is mentioned: D-ribose 5-phosphate to D-ribose 1-phosphate
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?
D-ribose 1-phosphate
D-ribose 5-phosphate
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only the reverse reaction is mentioned: D-ribose 5-phosphate to D-ribose 1-phosphate
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?
D-ribose 1-phosphate
D-ribose 5-phosphate
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-
-
?
Deoxyribose 1-phosphate
Deoxyribose 5-phosphate
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at 25% of the activity relative to ribose 1-phosphate
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-
?
additional information
?
-
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does not accept 2,3-dideoxyribose 5-phosphate as substrate
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-
?
additional information
?
-
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the enzyme is involved in the salvage pathway of nucleoside synthesis
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-
?
additional information
?
-
-
the enzyme is involved in the salvage pathway of nucleoside synthesis
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-
?
additional information
?
-
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Pgm3 functions as the major phosphoribomutase in vivo
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-
?
additional information
?
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-
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
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-
?
additional information
?
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trace levels of activity with glucose 1-phosphate and mannose 1-phosphate. No activity with fructose 1-phosphate, N-acetylglucosamine 1-phosphate and 3-phosphoglycerate
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-
?
additional information
?
-
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trace levels of activity with glucose 1-phosphate and mannose 1-phosphate. No activity with fructose 1-phosphate, N-acetylglucosamine 1-phosphate and 3-phosphoglycerate
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Ribose 1-phosphate
?
-
inducible enzyme. In order to enter the pentose phosphate cycle ribose 1-phosphate must be isomerized to ribose 5-phosphate
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-
?
alpha-D-ribose 1-phosphate
D-ribose 5-phosphate
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PPM is involve in the salvage pathway of nucleoside synthesis
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?
alpha-D-ribose 1-phosphate
D-ribose 5-phosphate
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-
-
?
additional information
?
-
-
the enzyme is involved in the salvage pathway of nucleoside synthesis
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-
?
additional information
?
-
-
the enzyme is involved in the salvage pathway of nucleoside synthesis
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-
?
additional information
?
-
-
Pgm3 functions as the major phosphoribomutase in vivo
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-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
-
activity is dependent on Mn2+, Ni2+ or Co2+. Optimal concentration: 0.05-0.06 mM
Mg2+
Mn2+
Ni2+
additional information
Mn2+
-
activity is dependent on Mn2+, Ni2+ or Co2+. Optimal concentration: 0.05-0.06 mM
Ni2+
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activity is dependent on Mn2+, Ni2+ or Co2+. Optimal concentration: 0.05 mM with deoxyribose 1-phosphate and 0.09 mM with ribose 1-phosphate as substrate
additional information
the presence of Ni2+, Co2+, Zn2+, and Cu2+ enhances enzyme activities, but not as much as Mn2+
additional information
-
the presence of Ni2+, Co2+, Zn2+, and Cu2+ enhances enzyme activities, but not as much as Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alpha-D-Glucose 1,6-bisphosphate
-
about 7fold increase of activity at 0.001 mM
Deoxyribose-1,5-diphosphate
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10fold stimulation, Km: 0.00017 mM, optimal concentration: 0.0014 mM
glucose 1,6-bisphosphate
required for activation. The conformational change in Lys240 alters the affinity of the enzyme for the activator
D-Glucose 1,6-bisphosphate
there is a concentration-dependent enhancement of PPM activity between 0.0001 mM and 0.0025 mM D-glucose 1,6-bisphosphate
glucose 1,6-diphosphate
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3fold stimulation, Km: 0.00008 mM, optimal concentration: 0.0007 mM
ribose-1,5-diphosphate
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10fold stimulation, Km: 0.00017 mM, optimal concentration: 0.0014 mM
ribose-1,5-diphosphate
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stimulates, Km: 0.00024 mM for enzyme form I, 0.00027 mM for enzyme form II and 0.00029 mM for enzyme form III
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.263
D-ribose 5-phosphate
in 25 mM Tris-HCl, pH 8.0, and 0.1 mM MnCl2, 0.0005 mM glucose 1,6-bisphosphate,at 23°C
0.5 - 3
alpha-D-ribose 1-phosphate
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recombinant His-tagged Pgm2, pH 7.5, 30°C
0.75
alpha-D-ribose 1-phosphate
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recombinant His-tagged Pgm3, pH 7.5, 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10.2
D-ribose 5-phosphate
in 25 mM Tris-HCl, pH 8.0, and 0.1 mM MnCl2, 0.0005 mM glucose 1,6-bisphosphate,at 23°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.5 - 8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8
about 40% activity at pH 6.5, more than 70% activity between pH 7.0 and 8.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65
90
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 100
about 30% activity at 30°C, about 40% activity at 40°C, about 50% activity at 50°C, about 60% activity at 60°C, about 70% activity at 70°C, about 80% activity at 80°C, 100% activity at 90°C, about 90% activity at 100°C
70 - 100
70°C: about 55% of maximal activity, 100°C: about 90% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
wild-type and regulatory mutants
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brenda