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2,3-dideoxyribose 5-phosphate
2,3-dideoxyribose 1-phosphate
2-deoxy-D-ribose 1-phosphate
2-deoxy-D-ribose 5-phosphate
-
-
-
?
2-deoxy-D-ribose 5-phosphate
2-deoxy-D-ribose 1-phosphate
2-deoxyribose 5-phosphate
2-deoxyribose 1-phosphate
2-Deoxyribose 5-phosphate
?
-
-
-
-
?
alpha-D-arabinose 5-phosphate
alpha-D-arabinose 1-phosphate
-
-
-
-
?
alpha-D-pentose 5-phosphate
alpha-D-pentose 1-phosphate
-
-
-
-
?
alpha-D-ribose 1-phosphate
alpha-D-ribose 5-phosphate
alpha-D-ribose 1-phosphate
D-ribose 5-phosphate
alpha-D-ribose 5-phosphate
alpha-D-ribose 1-phosphate
-
-
-
r
arabinose 5-phosphate
arabinose 1-phosphate
-
-
-
r
D-Arabinose 5-phosphate
D-Arabinose 1-phosphate
D-ribose 1-phosphate
D-ribose 5-phosphate
Deoxyribose 1-phosphate
Deoxyribose 5-phosphate
Glucose 1-phosphate
?
-
at 2.4% of the activity relative to ribose 1-phosphate
-
-
?
Ribose 1-phosphate
?
-
inducible enzyme. In order to enter the pentose phosphate cycle ribose 1-phosphate must be isomerized to ribose 5-phosphate
-
-
?
additional information
?
-
2,3-dideoxyribose 5-phosphate
2,3-dideoxyribose 1-phosphate
-
-
-
?, r
2,3-dideoxyribose 5-phosphate
2,3-dideoxyribose 1-phosphate
-
-
-
?
2-deoxy-D-ribose 5-phosphate
2-deoxy-D-ribose 1-phosphate
-
-
-
-
r
2-deoxy-D-ribose 5-phosphate
2-deoxy-D-ribose 1-phosphate
-
-
-
r
2-deoxyribose 5-phosphate
2-deoxyribose 1-phosphate
-
-
-
?
2-deoxyribose 5-phosphate
2-deoxyribose 1-phosphate
-
-
-
?
2-deoxyribose 5-phosphate
2-deoxyribose 1-phosphate
-
at 156% of the activity relative to ribose 5-phosphate
-
?
2-deoxyribose 5-phosphate
2-deoxyribose 1-phosphate
-
at 156% of the activity relative to ribose 5-phosphate
-
?
alpha-D-ribose 1-phosphate
alpha-D-ribose 5-phosphate
-
-
-
r
alpha-D-ribose 1-phosphate
alpha-D-ribose 5-phosphate
-
-
-
r
alpha-D-ribose 1-phosphate
alpha-D-ribose 5-phosphate
-
-
-
-
r
alpha-D-ribose 1-phosphate
alpha-D-ribose 5-phosphate
-
-
-
-
?
alpha-D-ribose 1-phosphate
alpha-D-ribose 5-phosphate
-
-
-
r
alpha-D-ribose 1-phosphate
D-ribose 5-phosphate
-
-
-
-
r
alpha-D-ribose 1-phosphate
D-ribose 5-phosphate
-
-
-
r
alpha-D-ribose 1-phosphate
D-ribose 5-phosphate
-
-
-
r
alpha-D-ribose 1-phosphate
D-ribose 5-phosphate
-
-
-
-
r
alpha-D-ribose 1-phosphate
D-ribose 5-phosphate
-
-
-
-
?
alpha-D-ribose 1-phosphate
D-ribose 5-phosphate
-
-
-
?
alpha-D-ribose 1-phosphate
D-ribose 5-phosphate
-
-
-
-
?
alpha-D-ribose 1-phosphate
D-ribose 5-phosphate
-
-
-
-
?
alpha-D-ribose 1-phosphate
D-ribose 5-phosphate
-
-
-
r
alpha-D-ribose 1-phosphate
D-ribose 5-phosphate
-
PPM is involve in the salvage pathway of nucleoside synthesis
-
?
alpha-D-ribose 1-phosphate
D-ribose 5-phosphate
-
-
-
?
alpha-D-ribose 1-phosphate
D-ribose 5-phosphate
-
-
-
?
D-Arabinose 5-phosphate
D-Arabinose 1-phosphate
-
-
-
-
?
D-Arabinose 5-phosphate
D-Arabinose 1-phosphate
-
at 8.61% of the activity relative to ribose 5-phosphate
-
-
?
D-Arabinose 5-phosphate
D-Arabinose 1-phosphate
-
at 8.61% of the activity relative to ribose 5-phosphate
-
-
?
D-ribose 1-phosphate
D-ribose 5-phosphate
-
-
-
?
D-ribose 1-phosphate
D-ribose 5-phosphate
-
-
-
-
?
D-ribose 1-phosphate
D-ribose 5-phosphate
-
only the reverse reaction is mentioned: D-ribose 5-phosphate to D-ribose 1-phosphate
-
-
?
D-ribose 1-phosphate
D-ribose 5-phosphate
-
only the reverse reaction is mentioned: D-ribose 5-phosphate to D-ribose 1-phosphate
-
?
D-ribose 1-phosphate
D-ribose 5-phosphate
-
only the reverse reaction is mentioned: D-ribose 5-phosphate to D-ribose 1-phosphate
-
?
D-ribose 1-phosphate
D-ribose 5-phosphate
-
-
-
?
D-ribose 1-phosphate
D-ribose 5-phosphate
-
-
-
?
Deoxyribose 1-phosphate
Deoxyribose 5-phosphate
-
-
-
-
?
Deoxyribose 1-phosphate
Deoxyribose 5-phosphate
-
-
-
-
?
Deoxyribose 1-phosphate
Deoxyribose 5-phosphate
-
at 25% of the activity relative to ribose 1-phosphate
-
-
?
additional information
?
-
-
does not accept 2,3-dideoxyribose 5-phosphate as substrate
-
-
?
additional information
?
-
-
the enzyme is involved in the salvage pathway of nucleoside synthesis
-
-
?
additional information
?
-
-
the enzyme is involved in the salvage pathway of nucleoside synthesis
-
-
?
additional information
?
-
-
Pgm3 functions as the major phosphoribomutase in vivo
-
-
?
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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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2-Deoxyribose 5-phosphate
?
-
-
-
-
?
alpha-D-ribose 1-phosphate
alpha-D-ribose 5-phosphate
alpha-D-ribose 1-phosphate
D-ribose 5-phosphate
alpha-D-ribose 5-phosphate
alpha-D-ribose 1-phosphate
-
-
-
r
Ribose 1-phosphate
?
-
inducible enzyme. In order to enter the pentose phosphate cycle ribose 1-phosphate must be isomerized to ribose 5-phosphate
-
-
?
additional information
?
-
alpha-D-ribose 1-phosphate
alpha-D-ribose 5-phosphate
-
-
-
r
alpha-D-ribose 1-phosphate
alpha-D-ribose 5-phosphate
-
-
-
r
alpha-D-ribose 1-phosphate
alpha-D-ribose 5-phosphate
-
-
-
-
?
alpha-D-ribose 1-phosphate
alpha-D-ribose 5-phosphate
-
-
-
r
alpha-D-ribose 1-phosphate
D-ribose 5-phosphate
-
-
-
-
?
alpha-D-ribose 1-phosphate
D-ribose 5-phosphate
-
-
-
?
alpha-D-ribose 1-phosphate
D-ribose 5-phosphate
-
-
-
-
?
alpha-D-ribose 1-phosphate
D-ribose 5-phosphate
-
-
-
-
?
alpha-D-ribose 1-phosphate
D-ribose 5-phosphate
-
PPM is involve in the salvage pathway of nucleoside synthesis
-
?
alpha-D-ribose 1-phosphate
D-ribose 5-phosphate
-
-
-
?
alpha-D-ribose 1-phosphate
D-ribose 5-phosphate
-
-
-
?
additional information
?
-
-
the enzyme is involved in the salvage pathway of nucleoside synthesis
-
-
?
additional information
?
-
-
the enzyme is involved in the salvage pathway of nucleoside synthesis
-
-
?
additional information
?
-
-
Pgm3 functions as the major phosphoribomutase in vivo
-
-
?
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Co2+
-
activity is dependent on Mn2+, Ni2+ or Co2+. Optimal concentration: 0.05-0.06 mM
Zn2+
1 mM, 45% of the activation with Mg2+
Mg2+
-
stimulates
Mg2+
-
optimal concentration 0.2 mM
Mg2+
1 mM, high activation
Mn2+
only Mn2+-incorporated enzyme shows significant enzyme activity
Mn2+
-
activity is dependent on Mn2+, Ni2+ or Co2+. Optimal concentration: 0.05-0.06 mM
Mn2+
-
highest activity at 0.1 mM
Mn2+
-
stimulates, optimal concentration is 0.2 mM
Mn2+
1 mM, 50% of the activation with Mg2+
Mn2+
required, 100% activity at 0.1 mM
Ni2+
-
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
Ni2+
1 mM, 70% of the activation with Mg2+
additional information
not dependent on Zn2+, Ni2+, Mg2+, and Co2+
additional information
-
not dependent on Zn2+, Ni2+, Mg2+, and Co2+
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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2-mercaptoethanol
100% activity at 0.5 mM
alpha-D-Glucose 1,6-bisphosphate
-
about 7fold increase of activity at 0.001 mM
alpha-D-glucose1,6-bisphosphate
-
D-Glucose 1,6-bisphosphate
D-glucose 1,6-diphosphate
-
-
Deoxyribose-1,5-diphosphate
-
10fold stimulation, Km: 0.00017 mM, optimal concentration: 0.0014 mM
dithiothreitol
100% activity at 0.5 mM
glucose 1,6-bisphosphate
required for activation. The conformational change in Lys240 alters the affinity of the enzyme for the activator
Cys
-
enhances activity, particularly in presence of Mg2+
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
D-Glucose 1,6-bisphosphate
-
required
glucose 1,6-diphosphate
-
3fold stimulation, Km: 0.00008 mM, optimal concentration: 0.0007 mM
glucose 1,6-diphosphate
-
required for maximal activity
glucose 1,6-diphosphate
-
activates, optimal concentration 0.01 mM
ribose-1,5-diphosphate
-
10fold stimulation, Km: 0.00017 mM, optimal concentration: 0.0014 mM
ribose-1,5-diphosphate
-
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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enzyme alone, co-crystallized with ribose 5-phosphate, co-crystallized with glucose 1,6-bisphosphate, and following activation with glucose 1,6-bisphosphate, hanging drop vapor diffusion method, using 100 mM Bis-Tris, pH 5.5, 50 mM MnCl2, 14% (w/v) polyethylene glycol 3350, and 75 mM NH4CH3COO
hanging drop vapor diffusion method, using 100 mM Bis-Tris pH 5.5, 50 mM MnCl2, 13-16% PEG 3350, and 25-100 mM NH4CH3COO
-
hanging drop vapor diffusion method, using 100 mM Bis-Tris pH 5.5, 50 mM MnCl2, 13-16% PEG 3350, and 25-100 mM NH4CH3COO
-
purified recombinant detagged wild-type and mutant T85Q and T85E enzymes free or in complex with glucose 1,6-bisphosphate, hanging drop vapor diffusion method, for the free enzyme crystals: mixing of 10 mg/ml protein in 25mM Tris-HCl, pH 7.5, and 1 mM MnCl2, with reservoir solution containing 100 mM Bis-Tris, pH 5.5, 50 mM MnCl2, 17% PEG 3350 (wild-type) or 13% PEG 3350 (mutant T85Q), and 75 mM NH4CH3COO, for the complex crystals: mixing of 10 mg/ml protein in 5 mM glucose 1,6-bisphosphate, 25 mM Tris-HCl, pH 7.4, and 1 mM MnCl2 with a reservoir solution containing 100 mM Bis-Tris, pH 5.5, 50 mM MnCl2, 14% PEG 3350, and 50 mM NH4CH3COO, X-ray diffraction structure determination and analysis at 1.8-2.3 A resolution
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D156A
site-directed mutagenesis, the D156A variant displays a dramatically reduced level of phosphorylation of the active site Thr85 compared to the wild-type, and does not acquire phosphatase activity
K240A
site-directed mutagenesis, the K240A variant can be phosphorylated by the small molecule activator glucose 1,6-bisphosphate like the wild-type enzyme
T85E
site-directed mutagenesis, the T85E variant mimics the active site charge of the activated state of the enzyme, the affinity for activator glucose 1,6-bisphosphate is 4.5fold reduced compared to the wild-type enzyme
T85Q
site-directed mutagenesis, the T85Q variant mimics the active site charge of the unactivated state of the enzyme, the affinity for activator glucose 1,6-bisphosphate is only slightly reduced compared to the wild-type enzyme
D156A
-
site-directed mutagenesis, the D156A variant displays a dramatically reduced level of phosphorylation of the active site Thr85 compared to the wild-type, and does not acquire phosphatase activity
-
K240A
-
site-directed mutagenesis, the K240A variant can be phosphorylated by the small molecule activator glucose 1,6-bisphosphate like the wild-type enzyme
-
T85E
-
site-directed mutagenesis, the T85E variant mimics the active site charge of the activated state of the enzyme, the affinity for activator glucose 1,6-bisphosphate is 4.5fold reduced compared to the wild-type enzyme
-
T85Q
-
site-directed mutagenesis, the T85Q variant mimics the active site charge of the unactivated state of the enzyme, the affinity for activator glucose 1,6-bisphosphate is only slightly reduced compared to the wild-type enzyme
-
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Kammen, H.O.; Koo, R.
Phosphopentomutases. I. Identification of two activities in rabbit tissues
J. Biol. Chem.
244
4888-4893
1969
Oryctolagus cuniculus
brenda
Hammer-Jespersen, K.; Munch-Petersen, A.
Phosphodeoxyribomutase from Escherichia coli. Purification and some properties
Eur. J. Biochem.
17
397-407
1970
Escherichia coli
brenda
Munch-Petersen, A.; Nygaard, R.; Hammer-Jespersen, K.; Fiil, N.
Mutants constitutive for nucleoside-catabolizing enzymes in Escherichia coli K12. Isolation characterization and mapping
Eur. J. Biochem.
27
208-215
1972
Escherichia coli
brenda
Nygaard, P.
Nucleoside-catabolizing enzymes in Salmonella typhimurium. Induction by ribonucleotides
Eur. J. Biochem.
36
267-272
1973
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Leer, J.C.; Hammer-Jespersen, K.
Multiple forms of phosphodeoxyribomutase from Escherichia coli. Physical and chemical characterization
Biochemistry
14
599-607
1975
Escherichia coli
brenda
Tozzi, M.G.; Catalani, R.; Ipata, P.L.; Mura, U.
A coupled optical enzyme assay of phosphomutase
Anal. Biochem.
123
265-269
1982
Escherichia coli
brenda
Ipata, P.L.; Sgarrella, F.; Catalani, R.; Tozzi, M.G.
Induction of phosphoribomutase in Bacillus cereus growing on nucleosides
Biochim. Biophys. Acta
755
253-256
1983
Bacillus cereus
brenda
Barsky, D.L.; Hoffee, P.A.
Purification and characterization of phosphopentomutase from rat liver
Biochim. Biophys. Acta
743
162-171
1983
Rattus norvegicus
brenda
Barbas, C.F.; Wong, C.H.
Overexpression and substrate specificity studies of phosphodeoxyribomutase and thymidine phosphorylase
Bioorg. Chem.
19
261-269
1991
Escherichia coli
-
brenda
Hamamoto, T.; Noguchi, T.; Midorikawa, Y.
Phosphopentomutase of Bacillus stearothermophilus TH6-2: the enzyme and its gene ppm
Biosci. Biotechnol. Biochem.
62
1103-1108
1998
Geobacillus stearothermophilus, Escherichia coli, Geobacillus stearothermophilus TH6-2
brenda
Rashid, N.; Imanaka, H.; Fukui, T.; Atomi, H.; Imanaka, T.
Presence of a novel phosphopentomutase and a 2-deoxyribose 5-phosphate aldolase reveals a metabolic link between pentoses and central carbon metabolism in the hyperthermophilic archaeon Thermococcus kodakaraensis
J. Bacteriol.
186
4185-4191
2004
Thermococcus kodakarensis (Q6I7B6), Thermococcus kodakarensis
brenda
Taverna-Porro, M.; Bouvier, L.A.; Pereira, C.A.; Montserrat, J.M.; Iribarren, A.M.
Chemoenzymic preparation of nucleosides from furanoses
Tetrahedron Lett.
49
2642-2645
2008
Escherichia coli
-
brenda
Horinouchi, N.; Kawano, T.; Sakai, T.; Matsumoto, S.; Sasaki, M.; Mikami, Y.; Ogawa, J.; Shimizu, S.
Screening and characterization of a phosphopentomutase useful for enzymatic production of 2-deoxyribonucleoside
N. Biotechnol.
26
75-82
2009
Lysinibacillus sphaericus (B3ITC5), Lysinibacillus sphaericus, Escherichia coli (P0A6K6), Escherichia coli, Lysinibacillus sphaericus AKU 229 (B3ITC5)
brenda
Panosian, T.D.; Nannemann, D.P.; Bachmann, B.O.; Iverson, T.M.
Crystallization and preliminary X-ray analysis of a phosphopentomutase from Bacillus cereus
Acta Crystallogr. Sect. F
66
811-814
2010
Bacillus cereus, Bacillus cereus ATCC 14579D
brenda
Panosian, T.D.; Nannemann, D.P.; Watkins, G.R.; Phelan, V.V.; McDonald, W.H.; Wadzinski, B.E.; Bachmann, B.O.; Iverson, T.M.
Bacillus cereus phosphopentomutase is an alkaline phosphatase family member that exhibits an altered entry point into the catalytic cycle
J. Biol. Chem.
286
8043-8054
2011
Bacillus cereus (Q818Z9), Bacillus cereus, Bacillus cereus ATCC 14579 (Q818Z9)
brenda
Iverson, T.M.; Panosian, T.D.; Birmingham, W.R.; Nannemann, D.P.; Bachmann, B.O.
Molecular differences between a mutase and a phosphatase: investigations of the activation step in Bacillus cereus phosphopentomutase
Biochemistry
51
1964-1975
2012
Bacillus cereus (Q818Z9), Bacillus cereus, Bacillus cereus DSM 31 (Q818Z9)
brenda
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
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586
4114-4118
2012
Saccharomyces cerevisiae
brenda
Moustafa, H.M.; Zaghloul, T.I.; Zhang, Y.H.
A simple assay for determining activities of phosphopentomutase from a hyperthermophilic bacterium Thermotoga maritima
Anal. Biochem.
501
75-81
2016
Thermotoga maritima (Q9WY14), Thermotoga maritima
brenda
Rivero, C.W.; De Benedetti, E.C.; Gallego, F.L.; Pessela, B.C.; Guisan, J.M.; Trelles, J.A.
Biosynthesis of an antiviral compound using a stabilized phosphopentomutase by multipoint covalent immobilization
J. Biotechnol.
249
34-41
2017
Escherichia coli, Escherichia coli ATCC 4157
brenda
Meyer, F.; Keller, P.; Hartl, J.; Groeninger, O.G.; Kiefer, P.; Vorholt, J.A.
Methanol-essential growth of Escherichia coli
Nat. Commun.
9
1508
2018
Escherichia coli, Escherichia coli MeSV1
brenda