BRENDA - Enzyme Database show
show all sequences of 6.1.1.26

N-Acetyl lysyl-tRNA synthetases evolved by a CcdB-based selection possess N-acetyl lysine specificity in vitro and in vivo

Umehara, T.; Kim, J.; Lee, S.; Guo, L.T.; Söll, D.; Park, H.S.; FEBS Lett. 586, 729-733 (2012)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
L301M/Y306L/C348S/A315V
while the wild type enzyme has a negligible charging activity for N-acetyl lysine, the mutant enzyme is able to acylate only N-acetyl lysine (not natural amino acids) onto tRNAPyl
Methanosarcina mazei
L301M/Y306L/L309A/C348F
while the wild type enzyme has a negligible charging activity for N-acetyl lysine, the mutant enzyme is able to acylate only N-acetyl lysine (not natural amino acids) onto tRNAPyl
Methanosarcina mazei
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
7.8
-
N-acetyl-L-lysine
pH and temperature not specified in the publication, mutant enzyme L301M/Y306L/C348S/A315V
Methanosarcina mazei
35.3
-
N-acetyl-L-lysine
pH and temperature not specified in the publication, mutant enzyme L301M/Y306L/L309A/C348F
Methanosarcina mazei
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + L-pyrrolysine + tRNAPyl
Methanosarcina mazei
-
AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
-
?
ATP + L-pyrrolysine + tRNAPyl
Methanosarcina mazei DSM 3647
-
AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Methanosarcina mazei
Q8PWY1
-
-
Methanosarcina mazei DSM 3647
Q8PWY1
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + L-pyrrolysine + tRNAPyl
-
727522
Methanosarcina mazei
AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
-
-
?
ATP + L-pyrrolysine + tRNAPyl
while the wild type enzyme has a negligible charging activity for N-acetyl-L-lysine, the mutant enzyme is able to acylate only N-acetyl-L-lysine (not natural amino acids) onto tRNAPyl
727522
Methanosarcina mazei
AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
-
-
?
ATP + L-pyrrolysine + tRNAPyl
-
727522
Methanosarcina mazei DSM 3647
AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
-
-
?
ATP + L-pyrrolysine + tRNAPyl
while the wild type enzyme has a negligible charging activity for N-acetyl-L-lysine, the mutant enzyme is able to acylate only N-acetyl-L-lysine (not natural amino acids) onto tRNAPyl
727522
Methanosarcina mazei DSM 3647
AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
-
-
?
ATP + N-acetyl-L-lysine + tRNAPyl
while the wild type enzyme has a negligible charging activity for N-acetyl-L-lysine, the mutant enzyme is able to acylate only N-acetyl-L-lysine (not natural amino acids) onto tRNAPyl
727522
Methanosarcina mazei
AMP + diphosphate + N-acetyl-L-lysyl-tRNAPyl
-
-
-
?
ATP + N-acetyl-L-lysine + tRNAPyl
while the wild type enzyme has a negligible charging activity for N-acetyl-L-lysine, the mutant enzyme is able to acylate only N-acetyl-L-lysine (not natural amino acids) onto tRNAPyl
727522
Methanosarcina mazei DSM 3647
AMP + diphosphate + N-acetyl-L-lysyl-tRNAPyl
-
-
-
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.00731
-
N-acetyl-L-lysine
pH and temperature not specified in the publication, mutant enzyme L301M/Y306L/C348S/A315V
Methanosarcina mazei
0.0323
-
N-acetyl-L-lysine
pH and temperature not specified in the publication, mutant enzyme L301M/Y306L/L309A/C348F
Methanosarcina mazei
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
L301M/Y306L/C348S/A315V
while the wild type enzyme has a negligible charging activity for N-acetyl lysine, the mutant enzyme is able to acylate only N-acetyl lysine (not natural amino acids) onto tRNAPyl
Methanosarcina mazei
L301M/Y306L/L309A/C348F
while the wild type enzyme has a negligible charging activity for N-acetyl lysine, the mutant enzyme is able to acylate only N-acetyl lysine (not natural amino acids) onto tRNAPyl
Methanosarcina mazei
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
7.8
-
N-acetyl-L-lysine
pH and temperature not specified in the publication, mutant enzyme L301M/Y306L/C348S/A315V
Methanosarcina mazei
35.3
-
N-acetyl-L-lysine
pH and temperature not specified in the publication, mutant enzyme L301M/Y306L/L309A/C348F
Methanosarcina mazei
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + L-pyrrolysine + tRNAPyl
Methanosarcina mazei
-
AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
-
?
ATP + L-pyrrolysine + tRNAPyl
Methanosarcina mazei DSM 3647
-
AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + L-pyrrolysine + tRNAPyl
-
727522
Methanosarcina mazei
AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
-
-
?
ATP + L-pyrrolysine + tRNAPyl
while the wild type enzyme has a negligible charging activity for N-acetyl-L-lysine, the mutant enzyme is able to acylate only N-acetyl-L-lysine (not natural amino acids) onto tRNAPyl
727522
Methanosarcina mazei
AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
-
-
?
ATP + L-pyrrolysine + tRNAPyl
-
727522
Methanosarcina mazei DSM 3647
AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
-
-
?
ATP + L-pyrrolysine + tRNAPyl
while the wild type enzyme has a negligible charging activity for N-acetyl-L-lysine, the mutant enzyme is able to acylate only N-acetyl-L-lysine (not natural amino acids) onto tRNAPyl
727522
Methanosarcina mazei DSM 3647
AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
-
-
?
ATP + N-acetyl-L-lysine + tRNAPyl
while the wild type enzyme has a negligible charging activity for N-acetyl-L-lysine, the mutant enzyme is able to acylate only N-acetyl-L-lysine (not natural amino acids) onto tRNAPyl
727522
Methanosarcina mazei
AMP + diphosphate + N-acetyl-L-lysyl-tRNAPyl
-
-
-
?
ATP + N-acetyl-L-lysine + tRNAPyl
while the wild type enzyme has a negligible charging activity for N-acetyl-L-lysine, the mutant enzyme is able to acylate only N-acetyl-L-lysine (not natural amino acids) onto tRNAPyl
727522
Methanosarcina mazei DSM 3647
AMP + diphosphate + N-acetyl-L-lysyl-tRNAPyl
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.00731
-
N-acetyl-L-lysine
pH and temperature not specified in the publication, mutant enzyme L301M/Y306L/C348S/A315V
Methanosarcina mazei
0.0323
-
N-acetyl-L-lysine
pH and temperature not specified in the publication, mutant enzyme L301M/Y306L/L309A/C348F
Methanosarcina mazei
Other publictions for EC 6.1.1.26
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)
726589
Yanagisawa. T.; Sumida
A novel crystal form of pyrrol ...
Methanosarcina mazei, Methanosarcina mazei DSM 3647
Acta Crystallogr. Sect. D
69
5-15
2013
-
-
-
1
-
-
-
-
-
-
-
-
-
6
-
-
1
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1
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1
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-
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-
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-
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-
727315
Lacey
Expanding the library and subs ...
Methanosarcina mazei
ChemBioChem
14
2100-2105
2013
-
-
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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1
1
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1
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1
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-
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727524
Ko
Pyrrolysyl-tRNA synthetase var ...
Escherichia coli
FEBS Lett.
587
3243-3248
2013
-
-
1
-
3
-
-
3
-
-
-
2
-
2
-
-
-
-
-
-
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-
3
-
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3
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1
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1
1
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3
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3
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2
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-
-
3
-
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3
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-
-
-
-
-
-
-
-
727525
Englert
Aminoacylation of tRNA 2'- or ...
Desulfitobacterium hafniense, Methanosarcina barkeri
FEBS Lett.
587
3360-3364
2013
-
-
-
-
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2
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2
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2
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727522
Umehara
N-Acetyl lysyl-tRNA synthetase ...
Methanosarcina mazei, Methanosarcina mazei DSM 3647
FEBS Lett.
586
729-733
2012
-
-
-
-
2
-
-
2
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2
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6
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6
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2
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2
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2
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2
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6
-
-
-
-
2
-
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-
727678
Wang
A rationally designed pyrrolys ...
Escherichia coli
J. Am. Chem. Soc.
134
2950-2953
2012
-
-
1
-
1
-
-
-
-
-
-
1
-
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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727925
Jiang
PylSn and the homologous N-ter ...
Desulfitobacterium hafniense, Methanosarcina barkeri
J. Biol. Chem.
287
32738-32746
2012
-
-
2
-
1
-
-
2
-
-
-
3
-
8
-
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2
-
-
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4
-
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3
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2
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2
2
-
1
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2
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3
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2
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-
4
-
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3
-
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-
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714264
Bhattacharyya
Probing the allosteric mechani ...
Desulfitobacterium hafniense
Biochemistry
50
6225-6236
2011
-
-
-
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2
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1
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1
1
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1
1
-
-
-
716190
Wang
The de novo engineering of pyr ...
Methanocaldococcus jannaschii, Methanosarcina mazei
Mol. Biosyst.
7
714-717
2011
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-
1
-
2
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2
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716337
Gaston
The complete biosynthesis of t ...
Methanosarcina barkeri
Nature
471
647-650
2011
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1
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3
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726549
Takimoto
Stereochemical basis for engin ...
Methanosarcina mazei, Methanosarcina mazei DSM 3647
ACS Chem. Biol.
6
733-743
2011
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1
1
2
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2
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6
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1
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2
1
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1
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1
1
2
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1
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2
1
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715267
Hancock
Expanding the genetic code of ...
Methanosarcina barkeri
J. Am. Chem. Soc.
132
14819-14824
2010
-
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1
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1
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1
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704197
Nguyen
Genetic encoding and labeling ...
Methanosarcina barkeri
J. Am. Chem. Soc.
131
8720-8721
2009
-
1
1
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1
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705880
Nozawa
Pyrrolysyl-tRNA synthetase-tRN ...
Desulfitobacterium hafniense
Nature
457
1163-1167
2009
-
-
-
1
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-
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-
-
5
-
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-
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1
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1
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1
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706527
Heinemann
The appearance of pyrrolysine ...
Methanosarcina acetivorans
Proc. Natl. Acad. Sci. USA
106
21103-21108
2009
-
-
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4
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1
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1
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1
1
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-
728142
Li
Specificity of pyrrolysyl-tRNA ...
Methanosarcina barkeri
J. Mol. Biol.
385
1156-1164
2009
-
-
-
-
-
-
-
4
-
-
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-
-
4
-
-
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-
-
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-
4
-
1
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4
1
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4
-
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-
-
4
-
1
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4
1
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-
-
-
-
-
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4
4
728143
Kobayashi
Recognition of non-alpha-amino ...
Methanosarcina mazei
J. Mol. Biol.
385
1352-1360
2009
-
1
1
1
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1
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5
-
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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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2
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690734
Mukai
Adding l-lysine derivatives to ...
Methanosarcina mazei
Biochem. Biophys. Res. Commun.
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818-822
2008
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690746
Lee
Structure of Desulfitobacteriu ...
Desulfitobacterium hafniense
Biochem. Biophys. Res. Commun.
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470-474
2008
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692360
Gundllapalli
Misacylation of pyrrolysine tR ...
Methanosarcina barkeri str. Fusaro
FEBS Lett.
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3353-3358
2008
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693638
Yanagisawa
Crystallographic studies on mu ...
Methanosarcina mazei
J. Mol. Biol.
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634-652
2008
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727286
Yanagisawa
Multistep engineering of pyrro ...
Methanosarcina mazei, Methanosarcina mazei DSM 3647
Chem. Biol.
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1187-1197
2008
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673691
Herring
The amino-terminal domain of p ...
Desulfitobacterium hafniense, Methanosarcina barkeri, Methanosarcina thermophila
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3197-3203
2007
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676083
Mahapatra
Class I and class II lysyl-tRN ...
Methanosarcina acetivorans
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1306-1318
2007
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676218
Herring
Recognition of pyrrolysine tRN ...
Desulfitobacterium hafniense
Nucleic Acids Res.
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1270-1278
2007
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676882
Kavran
Structure of pyrrolysyl-tRNA s ...
Methanosarcina mazei
Proc. Natl. Acad. Sci. USA
104
11268-11273
2007
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671091
Yanagisawa
Crystallization and preliminar ...
Methanosarcina mazei
Acta Crystallogr. Sect. F
62
1031-1033
2006
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673677
Polycarpo
Pyrrolysine analogues as subst ...
Methanosarcina barkeri
FEBS Lett.
580
6695-6700
2006
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676141
Blight
Direct charging of tRNA(CUA) w ...
Methanosarcina barkeri
Nature
431
333-335
2004
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676766
Polycarpo
An aminoacyl-tRNA synthetase t ...
Methanosarcina barkeri, Methanosarcina barkeri Fusaro
Proc. Natl. Acad. Sci. USA
101
12450-12454
2004
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