BRENDA - Enzyme Database
show all sequences of 2.7.2.1

Regulation of acetate kinase isozymes and its importance for mixed-acid fermentation in Lactococcus lactis

Puri, P.; Goel, A.; Bochynska, A.; Poolman, B.; J. Bacteriol. 196, 1386-1393 (2014)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
gene acka1, recombinant expression of His-tagged isozyme AckA1 in Escherichia coli strain MC1061; gene acka2, recombinant expression of His-tagged isozyme AckA2 in Escherichia coli strain MC1061
Lactococcus lactis
Inhibitors
Inhibitors
Commentary
Organism
Structure
ADP
competitive inhibition; competitive inhibition
Lactococcus lactis
D-fructose-1,6-bisphosphate
inhibits the activities of isozymes AckA1 and AckA2; inhibits the activities of isozymes AckA1 and AckA2
Lactococcus lactis
glyceraldehyde-3-phosphate
inhibits the activities of isozyme AckA1, but very poorly of isozyme AckA2; inhibits the activities of isozyme AckA1, but very poorly of isozyme AckA2
Lactococcus lactis
phospho-enol-pyruvate
PEP, a downstream intermediate of glycolysis, completely inhibits the activity of both enzymes at concentrations above 30 mM; PEP, a downstream intermediate of glycolysis, completely inhibits the activity of both enzymes at concentrations above 30 mM
Lactococcus lactis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
the turnover number of AckA1 is about an order of magnitude higher than that of AckA2 for the reaction in either direction. The Km values for acetyl phosphate, ATP, and ADP are similar for both isozymes. AckA2 has a higher affinity for acetate than does AckA1. Michaelis-Menten kinetics; the turnover number of AckA1 is about an order of magnitude higher than that of AckA2 for the reaction in either direction. The Km values for acetyl phosphate, ATP, and ADP are similar for both isozymes. AckA2 has a higher affinity for acetate than does AckA1. Michaelis-Menten kinetics
Lactococcus lactis
0.07
-
ATP
pH 7.5, 30C, recombinant His-tagged isozyme AckA1; pH 7.5, 30C, recombinant His-tagged isozyme AckA2
Lactococcus lactis
0.47
-
ADP
pH 7.5, 30C, recombinant His-tagged isozyme AckA1
Lactococcus lactis
0.54
-
acetyl phosphate
pH 7.5, 30C, recombinant His-tagged isozyme AckA1
Lactococcus lactis
0.55
-
acetyl phosphate
pH 7.5, 30C, recombinant His-tagged isozyme AckA2
Lactococcus lactis
0.74
-
ADP
pH 7.5, 30C, recombinant His-tagged isozyme AckA2
Lactococcus lactis
4.9
-
acetate
pH 7.5, 30C, recombinant His-tagged isozyme AckA2
Lactococcus lactis
20.54
-
acetate
pH 7.5, 30C, recombinant His-tagged isozyme AckA1
Lactococcus lactis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
K+
the enzyme requires monovalent K+ and divalent Mn2+or Mg2+ cations; the enzyme requires monovalent K+ and divalent Mn2+or Mg2+ cations
Lactococcus lactis
Mg2+
the enzyme requires monovalent K+ and divalent Mn2+or Mg2+ cations; the enzyme requires monovalent K+ and divalent Mn2+or Mg2+ cations
Lactococcus lactis
Mn2+
the enzyme requires monovalent K+ and divalent Mn2+or Mg2+ cations; the enzyme requires monovalent K+ and divalent Mn2+or Mg2+ cations
Lactococcus lactis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
ATP + acetate
Lactococcus lactis
-
ADP + acetyl phosphate
-
-
r
ATP + acetate
Lactococcus lactis MG1363
-
ADP + acetyl phosphate
-
-
r
Organism
Organism
UniProt
Commentary
Textmining
Lactococcus lactis
A2RNG4
gene acka2; isozyme AckA2 encoded by gene acka2
-
Lactococcus lactis
A2RNG5
gene acka1; isozyme AckA1 encoded by gene acka1
-
Lactococcus lactis MG1363
A2RNG4
gene acka2; isozyme AckA2 encoded by gene acka2
-
Lactococcus lactis MG1363
A2RNG5
gene acka1; isozyme AckA1 encoded by gene acka1
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant His-tagged isozyme AckA1 from Escherichia coli strain MC1061 by nickel affinity chromatography; recombinant His-tagged isozyme AckA2 from Escherichia coli strain MC1061 by nickel affinity chromatography
Lactococcus lactis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
ATP + acetate
-
738528
Lactococcus lactis
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
-
738528
Lactococcus lactis MG1363
ADP + acetyl phosphate
-
-
-
r
Synonyms
Synonyms
Commentary
Organism
ACK
-
Lactococcus lactis
AckA1
-
Lactococcus lactis
AckA2
-
Lactococcus lactis
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at; assay at
Lactococcus lactis
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
80
-
acetate
pH 7.5, 30C, recombinant His-tagged isozyme AckA2
Lactococcus lactis
93
-
acetyl phosphate
pH 7.5, 30C, recombinant His-tagged isozyme AckA2
Lactococcus lactis
761
-
acetate
pH 7.5, 30C, recombinant His-tagged isozyme AckA1
Lactococcus lactis
1105
-
acetyl phosphate
pH 7.5, 30C, recombinant His-tagged isozyme AckA1
Lactococcus lactis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at; assay at
Lactococcus lactis
Cofactor
Cofactor
Commentary
Organism
Structure
ADP
;
Lactococcus lactis
ATP
;
Lactococcus lactis
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
2.4
-
ADP
pH 7.5, 30C, recombinant His-tagged isozyme AckA1; pH 7.5, 30C, recombinant His-tagged isozyme AckA1
Lactococcus lactis
3.9
-
ADP
pH 7.5, 30C, recombinant His-tagged isozyme AckA2
Lactococcus lactis
4
-
glyceraldehyde-3-phosphate
pH 7.5, 30C, recombinant His-tagged isozyme AckA1; pH 7.5, 30C, recombinant His-tagged isozyme AckA1
Lactococcus lactis
15
-
phospho-enol-pyruvate
pH 7.5, 30C, recombinant His-tagged isozyme AckA1; pH 7.5, 30C, recombinant His-tagged isozyme AckA1
Lactococcus lactis
17
-
D-fructose-1,6-bisphosphate
pH 7.5, 30C, recombinant His-tagged isozyme AckA1; pH 7.5, 30C, recombinant His-tagged isozyme AckA1
Lactococcus lactis
18
-
phospho-enol-pyruvate
pH 7.5, 30C, recombinant His-tagged isozyme AckA2
Lactococcus lactis
43
-
D-fructose-1,6-bisphosphate
pH 7.5, 30C, recombinant His-tagged isozyme AckA2
Lactococcus lactis
Cloned(Commentary) (protein specific)
Commentary
Organism
gene acka1, recombinant expression of His-tagged isozyme AckA1 in Escherichia coli strain MC1061
Lactococcus lactis
gene acka2, recombinant expression of His-tagged isozyme AckA2 in Escherichia coli strain MC1061
Lactococcus lactis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
ADP
-
Lactococcus lactis
ATP
-
Lactococcus lactis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
ADP
competitive inhibition
Lactococcus lactis
D-fructose-1,6-bisphosphate
inhibits the activities of isozymes AckA1 and AckA2
Lactococcus lactis
glyceraldehyde-3-phosphate
inhibits the activities of isozyme AckA1, but very poorly of isozyme AckA2
Lactococcus lactis
phospho-enol-pyruvate
PEP, a downstream intermediate of glycolysis, completely inhibits the activity of both enzymes at concentrations above 30 mM
Lactococcus lactis
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
2.4
-
ADP
pH 7.5, 30C, recombinant His-tagged isozyme AckA1
Lactococcus lactis
3.9
-
ADP
pH 7.5, 30C, recombinant His-tagged isozyme AckA2
Lactococcus lactis
4
-
glyceraldehyde-3-phosphate
pH 7.5, 30C, recombinant His-tagged isozyme AckA1
Lactococcus lactis
15
-
phospho-enol-pyruvate
pH 7.5, 30C, recombinant His-tagged isozyme AckA1
Lactococcus lactis
17
-
D-fructose-1,6-bisphosphate
pH 7.5, 30C, recombinant His-tagged isozyme AckA1
Lactococcus lactis
18
-
phospho-enol-pyruvate
pH 7.5, 30C, recombinant His-tagged isozyme AckA2
Lactococcus lactis
43
-
D-fructose-1,6-bisphosphate
pH 7.5, 30C, recombinant His-tagged isozyme AckA2
Lactococcus lactis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
the turnover number of AckA1 is about an order of magnitude higher than that of AckA2 for the reaction in either direction. The Km values for acetyl phosphate, ATP, and ADP are similar for both isozymes. AckA2 has a higher affinity for acetate than does AckA1. Michaelis-Menten kinetics
Lactococcus lactis
0.07
-
ATP
pH 7.5, 30C, recombinant His-tagged isozyme AckA2
Lactococcus lactis
0.07
-
ATP
pH 7.5, 30C, recombinant His-tagged isozyme AckA1
Lactococcus lactis
0.47
-
ADP
pH 7.5, 30C, recombinant His-tagged isozyme AckA1
Lactococcus lactis
0.54
-
acetyl phosphate
pH 7.5, 30C, recombinant His-tagged isozyme AckA1
Lactococcus lactis
0.55
-
acetyl phosphate
pH 7.5, 30C, recombinant His-tagged isozyme AckA2
Lactococcus lactis
0.74
-
ADP
pH 7.5, 30C, recombinant His-tagged isozyme AckA2
Lactococcus lactis
4.9
-
acetate
pH 7.5, 30C, recombinant His-tagged isozyme AckA2
Lactococcus lactis
20.54
-
acetate
pH 7.5, 30C, recombinant His-tagged isozyme AckA1
Lactococcus lactis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
K+
the enzyme requires monovalent K+ and divalent Mn2+or Mg2+ cations
Lactococcus lactis
Mg2+
the enzyme requires monovalent K+ and divalent Mn2+or Mg2+ cations
Lactococcus lactis
Mn2+
the enzyme requires monovalent K+ and divalent Mn2+or Mg2+ cations
Lactococcus lactis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
ATP + acetate
Lactococcus lactis
-
ADP + acetyl phosphate
-
-
r
ATP + acetate
Lactococcus lactis MG1363
-
ADP + acetyl phosphate
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged isozyme AckA1 from Escherichia coli strain MC1061 by nickel affinity chromatography
Lactococcus lactis
recombinant His-tagged isozyme AckA2 from Escherichia coli strain MC1061 by nickel affinity chromatography
Lactococcus lactis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
ATP + acetate
-
738528
Lactococcus lactis
ADP + acetyl phosphate
-
-
-
r
ATP + acetate
-
738528
Lactococcus lactis MG1363
ADP + acetyl phosphate
-
-
-
r
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Lactococcus lactis
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
80
-
acetate
pH 7.5, 30C, recombinant His-tagged isozyme AckA2
Lactococcus lactis
93
-
acetyl phosphate
pH 7.5, 30C, recombinant His-tagged isozyme AckA2
Lactococcus lactis
761
-
acetate
pH 7.5, 30C, recombinant His-tagged isozyme AckA1
Lactococcus lactis
1105
-
acetyl phosphate
pH 7.5, 30C, recombinant His-tagged isozyme AckA1
Lactococcus lactis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Lactococcus lactis
General Information
General Information
Commentary
Organism
physiological function
acetate kinase converts acetyl phosphate to acetate along with the generation of ATP in the pathway for mixed-acid fermentation in Lactococcus lactis. The reverse reaction yields acetyl phosphate for assimilation purposes. AckA1 is an order of magnitude more active than AckA2 in both reaction directions, but AckA2 has the highest affinity for acetate. Allosteric regulation of isozymes AckA1 and AckA2 and the pool sizes of the glycolytic intermediates are consistent with a switch from homolactic to mixed-acid fermentation upon slowing of the growth rate; acetate kinase converts acetyl phosphate to acetate along with the generation of ATP in the pathway for mixed-acid fermentation in Lactococcus lactis. The reverse reaction yields acetyl phosphate for assimilation purposes. AckA1 is an order of magnitude more active than AckA2 in both reaction directions, but AckA2 has the highest affinity for acetate. Isozyme AckA2 has an important role under acetate-limiting conditions despite the lower activity. Allosteric regulation of isozymes AckA1 and AckA2 and the pool sizes of the glycolytic intermediates are consistent with a switch from homolactic to mixed-acid fermentation upon slowing of the growth rate
Lactococcus lactis
General Information (protein specific)
General Information
Commentary
Organism
physiological function
acetate kinase converts acetyl phosphate to acetate along with the generation of ATP in the pathway for mixed-acid fermentation in Lactococcus lactis. The reverse reaction yields acetyl phosphate for assimilation purposes. AckA1 is an order of magnitude more active than AckA2 in both reaction directions, but AckA2 has the highest affinity for acetate. Isozyme AckA2 has an important role under acetate-limiting conditions despite the lower activity. Allosteric regulation of isozymes AckA1 and AckA2 and the pool sizes of the glycolytic intermediates are consistent with a switch from homolactic to mixed-acid fermentation upon slowing of the growth rate
Lactococcus lactis
physiological function
acetate kinase converts acetyl phosphate to acetate along with the generation of ATP in the pathway for mixed-acid fermentation in Lactococcus lactis. The reverse reaction yields acetyl phosphate for assimilation purposes. AckA1 is an order of magnitude more active than AckA2 in both reaction directions, but AckA2 has the highest affinity for acetate. Allosteric regulation of isozymes AckA1 and AckA2 and the pool sizes of the glycolytic intermediates are consistent with a switch from homolactic to mixed-acid fermentation upon slowing of the growth rate
Lactococcus lactis
Other publictions for EC 2.7.2.1
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
Synonyms
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)
730304
Ingram-Smith
The role of active site residu ...
Methanosarcina thermophila
Life
5
861-871
2015
-
-
1
-
7
-
-
29
-
-
-
-
-
1
-
-
1
-
-
-
-
-
6
-
1
2
-
-
23
-
-
-
-
-
-
-
-
-
1
-
-
7
-
-
-
-
29
-
-
-
-
-
-
-
1
-
-
-
-
6
-
2
-
-
23
-
-
-
-
-
-
-
-
22
22
737465
Rozova
Acetate kinase-an enzyme of th ...
Methylomicrobium alcaliphilum 20Z, Methylomicrobium alcaliphilum
Antonie van Leeuwenhoek
108
965-974
2015
-
-
1
-
-
-
-
5
-
4
2
2
-
8
-
-
1
-
-
-
-
-
4
1
1
1
1
1
4
1
1
-
3
-
-
-
-
-
1
3
-
-
-
-
-
-
5
-
4
2
2
-
-
-
1
-
-
-
-
4
1
1
1
1
4
1
1
-
-
-
1
1
-
-
-
738863
Zhang
Enzymatic manufacture of deoxy ...
Escherichia coli
J. Microbiol. Biotechnol.
25
2034-2042
2015
-
-
1
-
1
-
-
-
-
1
-
1
-
3
-
-
-
-
-
-
-
-
1
-
2
1
-
-
-
1
-
-
2
-
-
-
-
-
1
2
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
746769
Rozova
Acetate kinase-an enzyme of t ...
Methylomicrobium alcaliphilum 20Z, Methylomicrobium alcaliphilum
Antonie van Leeuwenhoek
108
965-974
2015
-
-
1
-
-
-
-
2
-
3
3
-
-
8
-
-
1
-
-
-
-
-
4
1
1
1
2
1
2
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
2
-
3
3
-
-
-
-
1
-
-
-
-
4
1
1
2
1
2
1
-
-
-
-
-
-
-
2
2
727558
Welte
Experimental evidence of an ac ...
Methanosarcina mazei, Methanosarcina mazei DSM 3647
FEMS Microbiol. Lett.
359
147-153
2014
-
-
1
-
-
-
-
1
-
-
-
2
-
3
-
-
-
-
-
-
2
-
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
2
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
738528
Puri
Regulation of acetate kinase i ...
Lactococcus lactis, Lactococcus lactis MG1363
J. Bacteriol.
196
1386-1393
2014
-
-
1
-
-
-
4
8
-
3
-
4
-
5
-
-
1
-
-
-
-
-
4
-
4
1
-
-
4
1
-
-
2
7
-
-
-
-
2
4
-
-
-
-
8
11
10
-
6
-
4
-
-
-
2
-
-
-
-
4
-
2
-
-
4
2
-
-
-
-
1
2
-
-
-
738717
Yoshioka
Structural and mutational anal ...
Escherichia coli
J. Biosci. Bioeng.
118
502-507
2014
-
-
1
-
7
-
-
8
-
1
-
1
-
3
-
-
1
-
-
-
-
-
3
-
3
1
-
-
7
1
-
-
3
-
-
-
-
-
1
3
-
7
-
-
-
-
8
-
1
-
1
-
-
-
1
-
-
-
-
3
-
1
-
-
7
1
-
-
-
-
2
2
-
-
-
739218
Kushkevych
Acetate kinase activity and ki ...
Desulfomicrobium sp., Desulfomicrobium sp. Rod-9, Desulfovibrio piger, Desulfovibrio piger Vib-7
Open Microbiol. J.
8
138-143
2014
-
-
-
-
-
-
-
2
2
2
-
4
-
16
-
-
-
-
-
2
2
-
4
-
-
2
2
-
-
2
2
-
4
-
-
-
-
-
-
4
-
-
-
-
-
-
2
2
2
-
4
-
-
-
-
-
2
2
-
4
-
2
2
-
-
2
2
-
-
-
2
2
-
-
-
739591
Tang
Cold adaptation: structural an ...
Escherichia coli, Shewanella sp., Shewanella sp. AS-11
Protein J.
33
313-322
2014
-
-
2
-
-
-
-
30
-
3
6
3
-
6
-
-
2
-
-
-
-
-
7
2
3
2
-
2
32
2
-
-
4
-
-
-
-
-
2
4
-
-
-
-
-
-
30
-
3
6
3
-
-
-
2
-
-
-
-
7
2
2
-
2
32
2
-
-
-
-
5
5
-
32
32
723068
Thaker
Crystal structures of acetate ...
Cryptococcus neoformans, Entamoeba histolytica
J. Struct. Biol.
181
185-189
2013
-
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Winzer
-
Acetate kinase from Clostridiu ...
Clostridium acetobutylicum
Microbiology
143
3279-3286
1997
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1
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7
1
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642187
Diez-Gonzalez
The acetate kinase of Clostrid ...
Clostridium acetobutylicum, Clostridium acetobutylicum P262
Arch. Microbiol.
166
418-420
1996
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2
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1
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4
1
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642184
Aceti
-
Purification and characterizat ...
Methanosarcina thermophila
J. Biol. Chem.
249
15444-15448
1988
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2
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2
1
4
2
1
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8
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1
4
2
1
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1
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1
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1
1
8
1
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1
1
-
1
1
-
1
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642185
Kim
Inactivation of Acinetobacter ...
Acinetobacter calcoaceticus
Biochim. Biophys. Acta
956
103-109
1988
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1
2
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1
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642186
Mannens
-
Purification and immobilizatio ...
Desulfovibrio vulgaris
Biotechnol. Lett.
10
563-568
1988
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1
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1
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727804
Aceti
Purification and characterizat ...
Methanosarcina thermophila, Methanosarcina thermophila TM-1
J. Biol. Chem.
263
15444-15448
1988
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1
1
2
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4
3
2
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2
1
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1
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1
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1
14
1
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1
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1
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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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2
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4
3
2
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1
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1
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1
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1
14
1
1
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1
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1
1
-
1
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1
1
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-
-
642182
Fox
Isolation and characterization ...
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium LT2
J. Biol. Chem.
261
13487-13497
1986
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2
6
11
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4
3
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46
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2
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1
10
2
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2
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2
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6
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11
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3
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2
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1
10
2
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2
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642183
Vigenschow
Purification and properties of ...
Rhodopseudomonas palustris
Biol. Chem. Hoppe-Seyler
367
951-956
1986
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11
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2
4
1
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3
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1
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1
2
8
1
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1
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1
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1
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11
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2
4
1
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1
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1
2
8
1
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1
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1
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-
1
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642181
Ichikawa
-
Purification and properties of ...
Propionibacterium freudenreichii
J. Ferment. Technol.
63
143-149
1985
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6
-
6
2
1
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1
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1
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1
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5
1
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1
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1
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2
1
1
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6
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6
2
1
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1
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1
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5
1
1
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1
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2
1
1
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642179
Harwood
Properties of acetate kinase i ...
Spirochaeta sp., Spirochaeta sp. MA-2
J. Bacteriol.
152
246-254
1982
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6
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6
2
2
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2
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12
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6
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6
2
2
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12
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642180
Suzuki
-
Acetate kinase from Bacillus s ...
Geobacillus stearothermophilus, Geobacillus stearothermophilus NCA 1503
Methods Enzymol.
90
179-185
1982
3
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3
2
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13
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1
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1
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10
1
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1
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1
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642178
Nishimura
-
Acetate kinase from Veilonella ...
Veillonella parvula, Veillonella parvula 221 / ATCC 17745
Methods Enzymol.
71
311-316
1981
1
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2
2
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2
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1
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1
1
10
1
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2
2
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1
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1
1
10
1
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642177
Wong
Inactivation of Escherichia co ...
Escherichia coli
Biochim. Biophys. Acta
615
121-131
1980
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1
3
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1
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1
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642174
Griffith
Acetate kinase from Veillonell ...
Veillonella parvula
J. Biol. Chem.
254
442-446
1979
1
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5
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2
1
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2
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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
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1
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1
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1
1
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1
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642175
Griffith
Acetate kinase from Veillonell ...
Veillonella parvula
J. Biol. Chem.
254
6698-6702
1979
1
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4
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1
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1
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642176
Kahane
Purification and properties of ...
Acholeplasma laidlawii, Acholeplasma laidlawii oral
J. Bacteriol.
137
764-772
1979
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1
6
6
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1
5
2
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3
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1
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1
1
11
1
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5
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1
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6
-
6
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1
5
2
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1
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1
1
11
1
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5
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642172
Nakajima
Purification and properties of ...
Geobacillus stearothermophilus, Geobacillus stearothermophilus NCA 1503
J. Biochem.
84
193-203
1978
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1
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1
2
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6
3
2
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14
1
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1
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1
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11
1
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1
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1
1
1
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1
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1
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2
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6
3
2
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1
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1
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1
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11
1
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1
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1
1
1
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642173
Yoshimura
Purification and characterizat ...
Veillonella parvula
Arch. Biochem. Biophys.
189
424-432
1978
1
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9
4
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5
2
1
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3
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1
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1
2
5
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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9
-
4
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5
2
1
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1
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1
2
5
1
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-
1
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1
-
1
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-
-
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642171
Bowman
Acetate kinase from Veillonell ...
Veillonella parvula
J. Biol. Chem.
251
3117-3121
1976
1
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10
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2
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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10
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2
1
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1
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2
1
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642168
Janson
The inhibition of acetate, pyr ...
Escherichia coli
J. Biol. Chem.
249
2567-2571
1974
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2
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1
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1
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1
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642169
Janson
The specificity of chromium nu ...
Escherichia coli
J. Biol. Chem.
249
2572-2574
1974
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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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-
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642170
Schaupp
Purification and properties of ...
Moorella thermoacetica
Arch. Microbiol.
100
121-129
1974
-
-
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1
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1
1
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2
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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
1
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1
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1
-
1
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642167
Anthony
Exchange reactions catalyzed b ...
Escherichia coli
J. Biol. Chem.
246
6129-6135
1971
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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
1
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1
1
1
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1
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1
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1
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1
1
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-
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1
1
1
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642166
Rose
-
Acetate kinase ...
Escherichia coli, Lactobacillus delbrueckii, Streptococcus pyogenes
The Enzymes, 2nd. Ed. (Boyer, P. D. , Lardy, H. , Myrbaeck, K. , eds. )
6
115-118
1962
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1
3
4
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1
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3
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3
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2
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1
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7
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1
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1
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1
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3
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4
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1
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3
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2
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1
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7
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1
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1
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