BRENDA - Enzyme Database
show all sequences of 6.1.1.9

Functional group recognition at the aminoacylation and editing sites of E. coli valyl-tRNA synthetase

Tardif, K.D.; Horowitz, J.; RNA 10, 493-503 (2004)

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.002
-
L-valine
with mutant tRNAVal with 3'-terminal isoguanosine base analogue, pH 7.5, 37°C
Escherichia coli
0.0043
-
L-valine
with wild-type tRNAVal, pH 7.5, 37°C
Escherichia coli
0.0048
-
L-valine
with mutant tRNAVal with 3'-terminal inosine base analogue, pH 7.5, 37°C
Escherichia coli
0.005
-
L-valine
with mutant tRNAVal with 3'-terminal 2-aminopurine base analogue, pH 7.5, 37°C
Escherichia coli
0.0088
-
L-valine
with mutant tRNAVal with 3'-terminal purine riboside base analogue, pH 7.5, 37°C
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + L-valine + tRNAVal
Escherichia coli
-
AMP + diphosphate + L-valyl-tRNAVal
-
Escherichia coli
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
catalytic activity with L-valine and diverse tRNA analogues with functional group substitutions at the terminal nucleoside of the 3'-end, overview
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + L-valine + tRNAVal
-
653865
Escherichia coli
AMP + diphosphate + L-valyl-tRNAVal
-
653865
Escherichia coli
?
ATP + L-valine + tRNAVal,3' 2-aminopurine
mutant tRNAVal with 3'-terminal 2-aminopurine base analogue substitution
653865
Escherichia coli
AMP + diphosphate + L-valyl-tRNAVal, 3' 2-aminopurine
-
653865
Escherichia coli
?
ATP + L-valine + tRNAVal,3' inosine
mutant tRNAVal with 3'-terminal inosine base analogue substitution
653865
Escherichia coli
AMP + diphosphate + L-valyl-tRNAVal, 3' inosine
-
653865
Escherichia coli
?
ATP + L-valine + tRNAVal,3' isoguanosine
mutant tRNAVal with 3'-terminal isoguanosine base analogue substitution
653865
Escherichia coli
AMP + diphosphate + L-valyl-tRNAVal, 3' isoguanosine
-
653865
Escherichia coli
?
ATP + L-valine + tRNAVal,3' purine riboside
mutant tRNAVal with 3'-terminal purine riboside base analogue substitution
653865
Escherichia coli
AMP + diphosphate + L-valyl-tRNAVal, 3' purine riboside
-
653865
Escherichia coli
?
additional information
catalytic activity with L-valine and diverse tRNA analogues with functional group substitutions at the terminal nucleoside of the 3'-end, some of which stimulate the editing reaction, overview
653865
Escherichia coli
?
-
653865
Escherichia coli
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.68
-
L-valine
with mutant tRNAVal with 3'-terminal 2-aminopurine base analogue, pH 7.5, 37°C
Escherichia coli
0.99
-
L-valine
with mutant tRNAVal with 3'-terminal isoguanosine base analogue, pH 7.5, 37°C
Escherichia coli
1.06
-
L-valine
with mutant tRNAVal with 3'-terminal inosine base analogue, pH 7.5, 37°C
Escherichia coli
6.08
-
L-valine
with mutant tRNAVal with 3'-terminal 2-aminopurine base analogue, pH 7.5, 37°C; with mutant tRNAVal with 3'-terminal inosine base analogue, pH 7.5, 37°C; with mutant tRNAVal with 3'-terminal isoguanosine base analogue, pH 7.5, 37°C
Escherichia coli
13.9
-
L-valine
with wild-type tRNAVal, pH 7.5, 37°C
Escherichia coli
14.4
-
L-valine
with mutant tRNAVal with 3'-terminal purine riboside base analogue, pH 7.5, 37°C
Escherichia coli
Cofactor
Cofactor
Commentary
Organism
Structure
ATP
-
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
ATP
-
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.002
-
L-valine
with mutant tRNAVal with 3'-terminal isoguanosine base analogue, pH 7.5, 37°C
Escherichia coli
0.0043
-
L-valine
with wild-type tRNAVal, pH 7.5, 37°C
Escherichia coli
0.0048
-
L-valine
with mutant tRNAVal with 3'-terminal inosine base analogue, pH 7.5, 37°C
Escherichia coli
0.005
-
L-valine
with mutant tRNAVal with 3'-terminal 2-aminopurine base analogue, pH 7.5, 37°C
Escherichia coli
0.0088
-
L-valine
with mutant tRNAVal with 3'-terminal purine riboside base analogue, pH 7.5, 37°C
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + L-valine + tRNAVal
Escherichia coli
-
AMP + diphosphate + L-valyl-tRNAVal
-
Escherichia coli
?
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
catalytic activity with L-valine and diverse tRNA analogues with functional group substitutions at the terminal nucleoside of the 3'-end, overview
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + L-valine + tRNAVal
-
653865
Escherichia coli
AMP + diphosphate + L-valyl-tRNAVal
-
653865
Escherichia coli
?
ATP + L-valine + tRNAVal,3' 2-aminopurine
mutant tRNAVal with 3'-terminal 2-aminopurine base analogue substitution
653865
Escherichia coli
AMP + diphosphate + L-valyl-tRNAVal, 3' 2-aminopurine
-
653865
Escherichia coli
?
ATP + L-valine + tRNAVal,3' inosine
mutant tRNAVal with 3'-terminal inosine base analogue substitution
653865
Escherichia coli
AMP + diphosphate + L-valyl-tRNAVal, 3' inosine
-
653865
Escherichia coli
?
ATP + L-valine + tRNAVal,3' isoguanosine
mutant tRNAVal with 3'-terminal isoguanosine base analogue substitution
653865
Escherichia coli
AMP + diphosphate + L-valyl-tRNAVal, 3' isoguanosine
-
653865
Escherichia coli
?
ATP + L-valine + tRNAVal,3' purine riboside
mutant tRNAVal with 3'-terminal purine riboside base analogue substitution
653865
Escherichia coli
AMP + diphosphate + L-valyl-tRNAVal, 3' purine riboside
-
653865
Escherichia coli
?
additional information
catalytic activity with L-valine and diverse tRNA analogues with functional group substitutions at the terminal nucleoside of the 3'-end, some of which stimulate the editing reaction, overview
653865
Escherichia coli
?
-
653865
Escherichia coli
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.68
-
L-valine
with mutant tRNAVal with 3'-terminal 2-aminopurine base analogue, pH 7.5, 37°C
Escherichia coli
0.99
-
L-valine
with mutant tRNAVal with 3'-terminal isoguanosine base analogue, pH 7.5, 37°C
Escherichia coli
1.06
-
L-valine
with mutant tRNAVal with 3'-terminal inosine base analogue, pH 7.5, 37°C
Escherichia coli
6.08
-
L-valine
with mutant tRNAVal with 3'-terminal 2-aminopurine base analogue, pH 7.5, 37°C; with mutant tRNAVal with 3'-terminal inosine base analogue, pH 7.5, 37°C; with mutant tRNAVal with 3'-terminal isoguanosine base analogue, pH 7.5, 37°C
Escherichia coli
13.9
-
L-valine
with wild-type tRNAVal, pH 7.5, 37°C
Escherichia coli
14.4
-
L-valine
with mutant tRNAVal with 3'-terminal purine riboside base analogue, pH 7.5, 37°C
Escherichia coli
Other publictions for EC 6.1.1.9
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)
744977
Santamaria-Gomez
Sub-cellular localization and ...
Nostoc sp. PCC 7120
Front. Microbiol.
7
857
2016
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1
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1
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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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3
3
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746112
Wang
White panicle1, a Val-tRNA sy ...
Oryza sativa Japonica Group
Plant Physiol.
170
2110-2123
2016
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1
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1
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5
1
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4
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2
2
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745020
Rastogi
Caenorhabditis elegans glp-4 ...
Caenorhabditis elegans
G3 (Bethesda)
5
2719-2728
2015
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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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1
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3
3
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-
744659
Starosta
A conserved proline triplet i ...
Escherichia coli
Cell Rep.
9
476-483
2014
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1
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2
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1
3
3
1
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-
726908
Duarte
Defective valyl-tRNA synthetas ...
Neurospora crassa
Biochem. J.
448
297-306
2012
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1
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727910
Cvetesic
Kinetic partitioning between s ...
Escherichia coli
J. Biol. Chem.
287
25381-25394
2012
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715972
Li
Molecular trigger for pre-tran ...
Thermus thermophilus
J. Mol. Model.
17
555-564
2011
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1
1
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727894
Olmedo-Verd
Membrane anchoring of aminoacy ...
Anabaena sp., Anabaena sp. PCC 7120
J. Biol. Chem.
286
41057-41068
2011
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1
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5
1
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2
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22
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1
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8
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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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2
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1
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8
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1
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705623
Chiu
Schizosaccharomyces pombe poss ...
Schizosaccharomyces pombe
Mol. Biol. Evol.
27
1415-1424
2010
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1
2
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714322
Montanari
Aminoacyl-tRNA synthetases are ...
Homo sapiens
Biochim. Biophys. Acta
1803
1050-1057
2010
-
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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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715519
Dulic
Partitioning of tRNA-dependent ...
Escherichia coli
J. Biol. Chem.
285
23799-23809
2010
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1
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3
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5
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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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4
1
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1
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1
1
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3
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1
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1
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1
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1
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4
1
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1
1
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3
3
702702
Bharatham
Molecular dynamics simulation ...
Thermus thermophilus
Biophys. Chem.
143
34-43
2009
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1
1
2
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693165
Chang
Promoting the formation of an ...
Homo sapiens, Saccharomyces cerevisiae
J. Biol. Chem.
283
30699-30706
2008
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2
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5
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2
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2
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2
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2
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694436
Rorbach
Overexpression of human mitoch ...
Homo sapiens
Nucleic Acids Res.
36
3065-3074
2008
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673963
Massey
Basic faced alpha-helices are ...
Arabidopsis thaliana, Homo sapiens, Oryza sativa, Saccharomyces cerevisiae, Takifugu rubripes
In Silico Biol.
6
259-273
2006
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7
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5
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7
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5
5
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674764
Chang
Redundancy of non-AUG initiato ...
Saccharomyces cerevisiae
J. Biol. Chem.
281
7775-7783
2006
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1
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1
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661769
Jiang
Three-dimensional reconstructi ...
Homo sapiens
FEBS Lett.
579
6049-6054
2005
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662398
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Specific valylation of turnip ...
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Godar
Mammalian high molecular weigh ...
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Molecular cloning of the gene ...
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Colas
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Properties of purified chlorop ...
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The mechanism of inhibition of ...
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Natarajan
Purification and properties of ...
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The mitochondrial and cytoplas ...
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Valyl-tRNA, isoleucyl-tRNA and ...
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Paradies
Isolation and crystallization ...
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531
Bergmann
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The Enzymic synthesis of amino ...
Escherichia coli
J. Biol. Chem.
236
1735-1740
1961
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