BRENDA - Enzyme Database
show all sequences of 2.7.2.8

Site-directed mutagenesis and feedback-resistant N-acetyl-L-glutamate kinase (NAGK) increase Corynebacterium crenatum L-arginine production

Xu, M.; Rao, Z.; Dou, W.; Yang, J.; Jin, J.; Xu, Z.; Amino Acids 43, 255-266 (2012)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli
Corynebacterium crenatum
Engineering
Amino acid exchange
Commentary
Organism
E19R
Km and kcat (N-acetyl-L-glutamate) similar to wild-type, IC50 (L-arginine) approximately 55fold increased compared to wild-type
Corynebacterium crenatum
H268N
Km and kcat (N-acetyl-L-glutamate) similar to wild-type, IC50 (L-arginine) approximately 55fold increased compared to wild-type
Corynebacterium crenatum
H268N/H26E
Km and kcat (N-acetyl-L-glutamate) similar to wild-type, IC50 (L-arginine) 875fold increased compared to wild-type
Corynebacterium crenatum
H268N/H26E/E19R
Km and kcat (N-acetyl-L-glutamate) similar to wild-type, IC50 (L-arginine) 1960fold increased compared to wild-type
Corynebacterium crenatum
H26E
Km and kcat (N-acetyl-L-glutamate) similar to wild-type, IC50 (L-arginine) approximately 55fold increased compared to wild-type
Corynebacterium crenatum
Inhibitors
Inhibitors
Commentary
Organism
Structure
L-arginine
-
Corynebacterium crenatum
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.29
-
N-acetyl-L-glutamate
mutant H26E, pH 8.0, 37C
Corynebacterium crenatum
3.33
-
N-acetyl-L-glutamate
mutant E19R, pH 8.0, 37C
Corynebacterium crenatum
3.36
-
N-acetyl-L-glutamate
mutant H268N/H26E/E19R, pH 8.0, 37C
Corynebacterium crenatum
3.42
-
N-acetyl-L-glutamate
mutant H268N/H26E, pH 8.0, 37C; wild-type, pH 8.0, 37C
Corynebacterium crenatum
3.45
-
N-acetyl-L-glutamate
mutant H268N, pH 8.0, 37C
Corynebacterium crenatum
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36000
-
recombinant protein
Corynebacterium crenatum
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Corynebacterium crenatum
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + N-acetyl-L-glutamate
-
721268
Corynebacterium crenatum
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
?
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Corynebacterium crenatum
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
31.4
-
N-acetyl-L-glutamate
wild-type, pH 8.0, 37C, with 1 mM L-arginine
Corynebacterium crenatum
41
-
N-acetyl-L-glutamate
mutant H26E, pH 8.0, 37C, with 1 mM L-arginine
Corynebacterium crenatum
41.1
-
N-acetyl-L-glutamate
mutant H268N, pH 8.0, 37C, with 1 mM L-arginine
Corynebacterium crenatum
42
-
N-acetyl-L-glutamate
mutant E19R, pH 8.0, 37C, with 1 mM L-arginine
Corynebacterium crenatum
44.4
-
N-acetyl-L-glutamate
mutant H26E, pH 8.0, 37C
Corynebacterium crenatum
45.1
-
N-acetyl-L-glutamate
wild-type, pH 8.0, 37C
Corynebacterium crenatum
45.3
-
N-acetyl-L-glutamate
mutant H268N, pH 8.0, 37C
Corynebacterium crenatum
45.6
-
N-acetyl-L-glutamate
mutant H268N/H26E, pH 8.0, 37C, with 1 mM L-arginine
Corynebacterium crenatum
45.8
-
N-acetyl-L-glutamate
mutant E19R, pH 8.0, 37C
Corynebacterium crenatum
46
-
N-acetyl-L-glutamate
mutant H268N/H26E/E19R, pH 8.0, 37C, with 1 mM L-arginine
Corynebacterium crenatum
46.1
-
N-acetyl-L-glutamate
mutant H268N/H26E, pH 8.0, 37C
Corynebacterium crenatum
46.5
-
N-acetyl-L-glutamate
mutant H268N/H26E/E19R, pH 8.0, 37C
Corynebacterium crenatum
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Corynebacterium crenatum
IC50 Value
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.4
-
wild-type, pH 8.0, 37C
Corynebacterium crenatum
L-arginine
21
-
mutant H26E, pH 8.0, 37C
Corynebacterium crenatum
L-arginine
22
-
mutant H268N, pH 8.0, 37C
Corynebacterium crenatum
L-arginine
24
-
mutant E19R, pH 8.0, 37C
Corynebacterium crenatum
L-arginine
350
-
mutant H268N/H26E, pH 8.0, 37C
Corynebacterium crenatum
L-arginine
784
-
mutant H268N/H26E/E19R, pH 8.0, 37C
Corynebacterium crenatum
L-arginine
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli
Corynebacterium crenatum
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
E19R
Km and kcat (N-acetyl-L-glutamate) similar to wild-type, IC50 (L-arginine) approximately 55fold increased compared to wild-type
Corynebacterium crenatum
H268N
Km and kcat (N-acetyl-L-glutamate) similar to wild-type, IC50 (L-arginine) approximately 55fold increased compared to wild-type
Corynebacterium crenatum
H268N/H26E
Km and kcat (N-acetyl-L-glutamate) similar to wild-type, IC50 (L-arginine) 875fold increased compared to wild-type
Corynebacterium crenatum
H268N/H26E/E19R
Km and kcat (N-acetyl-L-glutamate) similar to wild-type, IC50 (L-arginine) 1960fold increased compared to wild-type
Corynebacterium crenatum
H26E
Km and kcat (N-acetyl-L-glutamate) similar to wild-type, IC50 (L-arginine) approximately 55fold increased compared to wild-type
Corynebacterium crenatum
IC50 Value (protein specific)
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.4
-
wild-type, pH 8.0, 37C
Corynebacterium crenatum
L-arginine
21
-
mutant H26E, pH 8.0, 37C
Corynebacterium crenatum
L-arginine
22
-
mutant H268N, pH 8.0, 37C
Corynebacterium crenatum
L-arginine
24
-
mutant E19R, pH 8.0, 37C
Corynebacterium crenatum
L-arginine
350
-
mutant H268N/H26E, pH 8.0, 37C
Corynebacterium crenatum
L-arginine
784
-
mutant H268N/H26E/E19R, pH 8.0, 37C
Corynebacterium crenatum
L-arginine
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
L-arginine
-
Corynebacterium crenatum
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.29
-
N-acetyl-L-glutamate
mutant H26E, pH 8.0, 37C
Corynebacterium crenatum
3.33
-
N-acetyl-L-glutamate
mutant E19R, pH 8.0, 37C
Corynebacterium crenatum
3.36
-
N-acetyl-L-glutamate
mutant H268N/H26E/E19R, pH 8.0, 37C
Corynebacterium crenatum
3.42
-
N-acetyl-L-glutamate
mutant H268N/H26E, pH 8.0, 37C; wild-type, pH 8.0, 37C
Corynebacterium crenatum
3.45
-
N-acetyl-L-glutamate
mutant H268N, pH 8.0, 37C
Corynebacterium crenatum
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36000
-
recombinant protein
Corynebacterium crenatum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + N-acetyl-L-glutamate
-
721268
Corynebacterium crenatum
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
?
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Corynebacterium crenatum
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
31.4
-
N-acetyl-L-glutamate
wild-type, pH 8.0, 37C, with 1 mM L-arginine
Corynebacterium crenatum
41
-
N-acetyl-L-glutamate
mutant H26E, pH 8.0, 37C, with 1 mM L-arginine
Corynebacterium crenatum
41.1
-
N-acetyl-L-glutamate
mutant H268N, pH 8.0, 37C, with 1 mM L-arginine
Corynebacterium crenatum
42
-
N-acetyl-L-glutamate
mutant E19R, pH 8.0, 37C, with 1 mM L-arginine
Corynebacterium crenatum
44.4
-
N-acetyl-L-glutamate
mutant H26E, pH 8.0, 37C
Corynebacterium crenatum
45.1
-
N-acetyl-L-glutamate
wild-type, pH 8.0, 37C
Corynebacterium crenatum
45.3
-
N-acetyl-L-glutamate
mutant H268N, pH 8.0, 37C
Corynebacterium crenatum
45.6
-
N-acetyl-L-glutamate
mutant H268N/H26E, pH 8.0, 37C, with 1 mM L-arginine
Corynebacterium crenatum
45.8
-
N-acetyl-L-glutamate
mutant E19R, pH 8.0, 37C
Corynebacterium crenatum
46
-
N-acetyl-L-glutamate
mutant H268N/H26E/E19R, pH 8.0, 37C, with 1 mM L-arginine
Corynebacterium crenatum
46.1
-
N-acetyl-L-glutamate
mutant H268N/H26E, pH 8.0, 37C
Corynebacterium crenatum
46.5
-
N-acetyl-L-glutamate
mutant H268N/H26E/E19R, pH 8.0, 37C
Corynebacterium crenatum
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Corynebacterium crenatum
General Information
General Information
Commentary
Organism
malfunction
argB gene coding the N-acetyl-L-glutamate kinase is first overexpressed in the strain SYPA5-5, whereas the L-arginine production is narrowly increased by 15.4%
Corynebacterium crenatum
General Information (protein specific)
General Information
Commentary
Organism
malfunction
argB gene coding the N-acetyl-L-glutamate kinase is first overexpressed in the strain SYPA5-5, whereas the L-arginine production is narrowly increased by 15.4%
Corynebacterium crenatum
Other publictions for EC 2.7.2.8
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)
738801
Zhao
Controlling the transcription ...
Corynebacterium crenatum, Corynebacterium crenatum SYPA5-5
J. Ind. Microbiol. Biotechnol.
43
55-66
2016
-
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1
-
8
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1
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1
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2
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4
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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
1
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8
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1
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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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1
1
-
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735596
Zhao
Structure of N-acetyl-L-glutam ...
Maricaulis maris, Maricaulis maris MCS10, Xanthomonas campestris, Xanthomonas campestris 8004
Biochem. Biophys. Res. Commun.
437
585-590
2013
-
-
2
1
10
-
2
-
-
1
-
4
-
7
-
-
2
1
-
-
7
-
6
-
2
-
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-
2
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2
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2
2
1
10
-
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2
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1
-
4
-
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2
-
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7
-
6
-
2
-
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-
2
-
-
-
-
3
3
-
-
-
721268
Xu
Site-directed mutagenesis and ...
Corynebacterium crenatum
Amino Acids
43
255-266
2012
-
-
1
-
5
-
1
5
-
-
1
-
-
1
-
-
-
-
-
-
-
-
1
-
1
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12
1
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-
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-
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6
-
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1
-
-
5
-
6
1
-
5
-
-
1
-
-
-
-
-
-
-
-
-
1
-
1
-
-
12
1
-
-
-
-
1
1
-
-
-
722087
Xu
Site-directed mutagenesis stud ...
Corynebacterium glutamicum
Curr. Microbiol.
64
164-172
2012
-
-
1
-
16
-
1
17
-
-
1
-
-
2
-
-
1
-
-
-
-
-
1
-
-
-
-
32
-
-
-
-
-
-
17
-
-
1
-
-
16
-
17
1
-
17
-
-
1
-
-
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-
1
-
-
-
-
1
-
-
-
-
32
-
-
-
-
-
-
-
-
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-
723557
de Cima
Insight on an arginine synthes ...
Saccharomyces cerevisiae
PLoS ONE
7
e34734
2012
-
-
1
1
1
-
1
4
-
-
-
-
-
4
-
-
1
-
-
-
-
-
1
1
1
-
-
4
-
-
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-
1
-
2
-
-
1
-
1
1
-
2
1
1
4
-
-
-
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-
1
-
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-
-
1
1
1
-
-
4
-
-
-
-
-
-
-
-
-
-
720845
Shi
A novel N-acetylglutamate synt ...
Maricaulis maris
PLoS ONE
6
e28825
2011
1
-
1
1
3
-
-
-
-
-
-
-
-
7
-
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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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1
3
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1
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1
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1
1
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723511
Marcos
Changes in dynamics upon oligo ...
Escherichia coli
PLoS Comput. Biol.
7(9)
e1002201
2011
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1
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722963
Fokina
A novel signal transduction pr ...
Synechococcus elongatus
J. Mol. Biol.
399
410-421
2010
-
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1
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7
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1
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1
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722965
Gil-Ortiz
Two crystal structures of Esch ...
Escherichia coli
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476-490
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-
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1
1
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4
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2
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1
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1
1
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4
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1
1
1
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1
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-
-
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702066
Feria Bourrellier
Metabolite regulation of the i ...
Arabidopsis thaliana
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387
700-704
2009
-
-
1
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1
1
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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1
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2
1
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704614
Min
Mechanism of allosteric inhibi ...
Arabidopsis thaliana, Pseudomonas aeruginosa
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2
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705148
Beez
N-acetyl-L-glutamate kinase (N ...
Arabidopsis thaliana, Synechococcus elongatus
J. Mol. Biol.
389
748-758
2009
2
-
2
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3
9
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2
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7
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2
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2
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5
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2
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4
2
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2
2
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4
3
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9
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2
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2
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2
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5
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5
5
689895
Wu
Protein preparation, crystalli ...
Streptococcus mutans
Protein Pept. Lett.
15
541-543
2008
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1
1
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