BRENDA - Enzyme Database show
show all sequences of 5.4.2.7

Multiple forms of phosphodeoxyribomutase from Escherichia coli. Physical and chemical characterization

Leer, J.C.; Hammer-Jespersen, K.; Biochemistry 14, 599-607 (1975)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
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
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.014
-
deoxyribose 1-phosphate
enzyme form I
Escherichia coli
0.015
-
deoxyribose 1-phosphate
enzyme form II
Escherichia coli
0.022
-
deoxyribose 1-phosphate
enzyme form III
Escherichia coli
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
45000
-
equilibrium centrifugation
Escherichia coli
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Purification (Commentary)
Commentary
Organism
multiple forms: I, II, II-1 and III-2
Escherichia coli
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
142
-
-
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-ribose 1-phosphate
-
3343
Escherichia coli
D-ribose 5-phosphate
-
-
-
-
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
25
-
half-life of the cobalt-enzyme in 1 mM EDTA: 15 min for enzyme form I, 31 min for enzyme form II
Escherichia coli
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
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
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.014
-
deoxyribose 1-phosphate
enzyme form I
Escherichia coli
0.015
-
deoxyribose 1-phosphate
enzyme form II
Escherichia coli
0.022
-
deoxyribose 1-phosphate
enzyme form III
Escherichia coli
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
45000
-
equilibrium centrifugation
Escherichia coli
Purification (Commentary) (protein specific)
Commentary
Organism
multiple forms: I, II, II-1 and III-2
Escherichia coli
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
142
-
-
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-ribose 1-phosphate
-
3343
Escherichia coli
D-ribose 5-phosphate
-
-
-
-
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
25
-
half-life of the cobalt-enzyme in 1 mM EDTA: 15 min for enzyme form I, 31 min for enzyme form II
Escherichia coli
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
1
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1
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1
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6
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1
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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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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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1
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2
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2
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2
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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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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
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2
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3
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1
1
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2
1
1
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1
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1
4
1
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1
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1
1
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2
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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2
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1
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1
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3
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3
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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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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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1
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1
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705839
Horinouchi
Screening and characterization ...
Escherichia coli, Lysinibacillus sphaericus, Lysinibacillus sphaericus AKU 229
N. Biotechnol.
26
75-82
2009
-
1
2
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1
2
3
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6
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3
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695174
Taverna-Porro
-
Chemoenzymic preparation of nu ...
Escherichia coli
Tetrahedron Lett.
49
2642-2645
2008
1
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1
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1
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1
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662012
Rashid
Presence of a novel phosphopen ...
Thermococcus kodakarensis
J. Bacteriol.
186
4185-4191
2004
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1
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1
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1
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5
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1
1
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1
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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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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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3
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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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3347
Barbas
-
Overexpression and substrate s ...
Escherichia coli
Bioorg. Chem.
19
261-269
1991
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1
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4
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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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1
1
2
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2
2
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2
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1
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1
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1
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3344
Tozzi
A coupled optical enzyme assay ...
Escherichia coli
Anal. Biochem.
123
265-269
1982
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3343
Leer
Multiple forms of phosphodeoxy ...
Escherichia coli
Biochemistry
14
599-607
1975
1
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3
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1
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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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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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1
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3
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7
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2
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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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