BRENDA - Enzyme Database show
show all sequences of 5.4.2.7

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

Rashid, N.; Imanaka, H.; Fukui, T.; Atomi, H.; Imanaka, T.; J. Bacteriol. 186, 4185-4191 (2004)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Thermococcus kodakarensis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.5
-
2-deoxy-D-ribose 1-phosphate
90°C
Thermococcus kodakarensis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
1 mM, high activation
Thermococcus kodakarensis
Mn2+
1 mM, 50% of the activation with Mg2+
Thermococcus kodakarensis
Ni2+
1 mM, 70% of the activation with Mg2+
Thermococcus kodakarensis
Zn2+
1 mM, 45% of the activation with Mg2+
Thermococcus kodakarensis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
210000
-
gel filtration
Thermococcus kodakarensis
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Thermococcus kodakarensis
Q6I7B6
KOD1
-
Purification (Commentary)
Commentary
Organism
partial
Thermococcus kodakarensis
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
210
-
-
Thermococcus kodakarensis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-deoxy-D-ribose 1-phosphate
-
662012
Thermococcus kodakarensis
2-deoxy-D-ribose 5-phosphate
-
-
-
?
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
662012
Thermococcus kodakarensis
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
tetramer
-
Thermococcus kodakarensis
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
90
-
-
Thermococcus kodakarensis
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
70
100
70°C: about 55% of maximal activity, 100°C: about 90% of maximal activity
Thermococcus kodakarensis
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
100
-
half-life: 90 min
Thermococcus kodakarensis
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
173
-
2-deoxy-D-ribose 1-phosphate
90°C
Thermococcus kodakarensis
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Thermococcus kodakarensis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.5
-
2-deoxy-D-ribose 1-phosphate
90°C
Thermococcus kodakarensis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
1 mM, high activation
Thermococcus kodakarensis
Mn2+
1 mM, 50% of the activation with Mg2+
Thermococcus kodakarensis
Ni2+
1 mM, 70% of the activation with Mg2+
Thermococcus kodakarensis
Zn2+
1 mM, 45% of the activation with Mg2+
Thermococcus kodakarensis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
210000
-
gel filtration
Thermococcus kodakarensis
Purification (Commentary) (protein specific)
Commentary
Organism
partial
Thermococcus kodakarensis
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
210
-
-
Thermococcus kodakarensis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-deoxy-D-ribose 1-phosphate
-
662012
Thermococcus kodakarensis
2-deoxy-D-ribose 5-phosphate
-
-
-
?
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
662012
Thermococcus kodakarensis
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
-
Thermococcus kodakarensis
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
90
-
-
Thermococcus kodakarensis
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
70
100
70°C: about 55% of maximal activity, 100°C: about 90% of maximal activity
Thermococcus kodakarensis
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
100
-
half-life: 90 min
Thermococcus kodakarensis
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
173
-
2-deoxy-D-ribose 1-phosphate
90°C
Thermococcus kodakarensis
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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3
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2
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2
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2
-
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748271
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Biosynthesis of an antiviral ...
Escherichia coli, Escherichia coli ATCC 4157
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1
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1
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1
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1
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2
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6
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1
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-
-
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2
1
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1
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1
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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
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2
1
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1
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-
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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
-
2
-
4
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1
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-
-
2
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2
1
1
1
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2
1
1
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3
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1
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-
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-
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2
-
2
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2
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1
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2
-
2
1
1
1
-
2
1
1
-
-
-
-
-
-
2
2
726977
Iverson
Molecular differences between ...
Bacillus cereus, Bacillus cereus DSM 31
Biochemistry
51
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2012
1
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1
1
4
1
-
-
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1
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2
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3
-
1
1
-
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2
1
1
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1
-
-
-
-
-
-
1
-
1
-
1
4
1
-
-
-
-
-
1
-
2
-
-
1
1
-
-
-
-
2
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-
727521
Walther
The PGM3 gene encodes the majo ...
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FEBS Lett.
586
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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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1
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-
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3
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3
-
1
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1
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1
-
1
-
-
-
-
-
-
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2
-
1
-
2
-
-
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1
-
-
3
-
3
-
1
-
-
-
1
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-
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1
1
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715660
Panosian
Bacillus cereus phosphopentomu ...
Bacillus cereus, Bacillus cereus ATCC 14579
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2011
1
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1
1
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3
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1
1
-
-
-
-
-
2
1
-
-
-
1
-
-
-
-
-
-
-
1
-
1
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1
-
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1
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2
1
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1
1
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2
1
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-
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1
-
-
-
-
-
-
-
-
-
-
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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-
-
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1
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4
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-
1
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-
-
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2
1
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1
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1
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1
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1
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2
1
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-
705839
Horinouchi
Screening and characterization ...
Escherichia coli, Lysinibacillus sphaericus, Lysinibacillus sphaericus AKU 229
N. Biotechnol.
26
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2009
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1
2
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1
2
3
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6
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3
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1
2
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-
-
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1
2
3
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3
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695174
Taverna-Porro
-
Chemoenzymic preparation of nu ...
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1
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-
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-
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1
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1
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-
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5
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1
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1
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1
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-
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1
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-
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5
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
662012
Rashid
Presence of a novel phosphopen ...
Thermococcus kodakarensis
J. Bacteriol.
186
4185-4191
2004
-
-
1
-
-
-
-
1
-
4
1
-
-
5
-
-
1
-
-
-
1
-
2
1
1
1
1
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
4
1
-
-
-
-
1
-
-
1
-
2
1
1
1
1
1
-
-
-
-
-
-
-
-
-
-
3348
Hamamoto
Phosphopentomutase of Bacillus ...
Escherichia coli, Geobacillus stearothermophilus, Geobacillus stearothermophilus TH6-2
Biosci. Biotechnol. Biochem.
62
1103-1108
1998
-
-
1
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3
3
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5
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1
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1
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18
2
2
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4
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1
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1
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1
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1
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-
-
-
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3
3
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1
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1
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18
2
2
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4
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1
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1
1
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Barbas
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Overexpression and substrate s ...
Escherichia coli
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1991
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4
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1
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1
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4
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3345
Ipata
Induction of phosphoribomutase ...
Bacillus cereus
Biochim. Biophys. Acta
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1983
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2
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Barsky
Purification and characterizat ...
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1983
2
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2
1
1
3
1
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1
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1
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2
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1
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1
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2
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2
2
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1
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2
1
1
3
1
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1
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1
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-
3344
Tozzi
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Leer
Multiple forms of phosphodeoxy ...
Escherichia coli
Biochemistry
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1
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3
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1
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Nygaard
Nucleoside-catabolizing enzyme ...
Salmonella enterica subsp. enterica serovar Typhimurium
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-
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1
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1
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1
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3341
Munch-Petersen
Mutants constitutive for nucle ...
Escherichia coli
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27
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1972
-
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1
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1
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1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
3340
Hammer-Jespersen
Phosphodeoxyribomutase from Es ...
Escherichia coli
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17
397-407
1970
3
-
-
-
-
-
7
2
-
3
2
-
-
2
-
-
1
-
-
-
1
-
2
1
-
-
-
-
1
-
-
-
-
-
-
3
-
-
-
-
-
-
-
7
-
2
-
3
2
-
-
-
-
1
-
-
1
-
2
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
3339
Kammen
Phosphopentomutases. I. Identi ...
Oryctolagus cuniculus
J. Biol. Chem.
244
4888-4893
1969
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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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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