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Information on EC 6.1.1.26 - pyrrolysine-tRNAPyl ligase and Organism(s) Methanosarcina barkeri and UniProt Accession Q6WRH6
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6.1.1.26 pyrrolysine-tRNAPyl ligaseIUBMB Comments
In organisms such as Methanosarcina barkeri that incorporate the modified amino acid pyrrolysine (Pyl) into certain methylamine methyltransferases, an unusual tRNAPyl, with a CUA anticodon, can be charged directly with pyrrolysine by this class II aminoacyl---tRNA ligase. The enzyme is specific for pyrrolysine as substrate as it cannot be replaced by lysine or any of the other natural amino acids .
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Word Map
- 6.1.1.26
- synthetases
- methanosarcina
-
amber
- aminoacylation
- mazei
-
ncaas
-
anticodon
-
aarss
- barkeri
-
pylts
-
histidyl-trnas
- hisrs
- hafniense
- desulfitobacterium
- methanosarcinaceae
-
trnacua
- phers
- phenylalanyl-trna
- seryl-trna
-
non-cognate
- glyrs
- molecular biology
- synthesis
The taxonomic range for the selected organisms is: Methanosarcina barkeri
The expected taxonomic range for this enzyme is: Bacteria, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
pylrs, pyrrolysyl-trna synthetase, class ii aminoacyl-trna synthetase, pylsn, lysz-rs, pylsc, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
pyrrolysyl-tRNA synthetase
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
L-pyrrolysine:tRNAPyl ligase (AMP-forming)
In organisms such as Methanosarcina barkeri that incorporate the modified amino acid pyrrolysine (Pyl) into certain methylamine methyltransferases, an unusual tRNAPyl, with a CUA anticodon, can be charged directly with pyrrolysine by this class II aminoacyl---tRNA ligase. The enzyme is specific for pyrrolysine as substrate as it cannot be replaced by lysine or any of the other natural amino acids [1].
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 2-amino-6-((R)-tetrahydrofuran-2-carboxamido)hexanoic acid + tRNAPyl
AMP + diphosphate + 2-amino-6-((R)-tetrahydrofuran-2-carboxamido)hexanoyl-tRNAPyl
-
catalytic efficiency (kcat/Km) is 9% of the catalytic efficiency for L-pyrrolysine
-
-
?
ATP + 2-amino-6-(cyclopentanecarboxamido)hexanoic acid + tRNAPyl
AMP + diphosphate + 2-amino-6-(cyclopentanecarboxamido)hexanoyl-tRNAPyl
-
catalytic efficiency (kcat/Km) is 0.3% of the catalytic efficiency for L-pyrrolysine
-
-
?
ATP + N-epsilon-cyclopentyloxycarbonyl-L-lysine + tRNAPyl
AMP + diphosphate + N-epsilon-cyclopentyloxycarbonyl-L-lysyl-tRNAPyl
-
-
-
-
?
ATP + N-epsilon-D-prolyl-L-lysine + tRNAPyl
AMP + diphosphate + N-epsilon-D-prolyl-L-lysyl-tRNAPyl
-
-
-
-
?
ATP + Nepsilon-cyclopentyloxycarbonyl-L-lysine + tRNAPyl
AMP + diphosphate + Nepsilon-cyclopentyloxycarbonyl-L-lysyl-tRNAPyl
-
catalytic efficiency (kcat/Km) is 1.8% of the catalytic efficiency for L-pyrrolysine
-
-
?
ATP + L-pyrrolysine + tRNAPyl
AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
-
-
?
ATP + L-pyrrolysine + tRNAPyl
AMP + diphosphate + L-pyrrolysyl-tRNAPyl
the N-terminal region of PylS influences complex formation with tRNAPyl
-
-
?
ATP + L-pyrrolysine + tRNAPyl
AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
-
-
-
?
ATP + L-pyrrolysine + tRNAPyl
AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
-
-
?
ATP + L-pyrrolysine + tRNAPyl
AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
-
-
-
?
ATP + L-pyrrolysine + tRNAPyl
AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
direct charging of tRNA(CUA) with pyrrolysine in vitro and in vivo
-
-
?
ATP + L-pyrrolysine + tRNAPyl
AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
Pyl-tRNAPyl insertion at UAG, a specialized mRNA motif is not essential for stopcodon recoding, unlike for selenocysteine incorporation
-
-
?
ATP + L-pyrrolysine + tRNAPyl
AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
direct charging of tRNA(CUA), isolated from Methanosarcina acetivorans strain C2A, with pyrrolysine in vitro and in vivo, PylS activates pyrrolysine with ATP and ligates pyrrolysine to tRNACUA in vitro in reactions specific for pyrrolysine
-
-
?
ATP + L-pyrrolysine + tRNAPyl
AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
the archaeal enzyme does not distinguish between archaeal and bacterial tRNAPyl species, substrate specificity, overview, residues from the PylRS amino-terminal domain affect activity in vivo
-
-
?
ATP + L-pyrrolysine + tRNAPyl
AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
the enzyme uses a special amber suppressor tRNA, tRNAPyl, that presumably recognizes this UAG codon, and does not accept L-lysine or tRNALys as substrates, direct transfer of L-pyrroslysine to the UAG codon of tRNAPyl, overview
-
-
?
ATP + L-pyrrolysine + tRNAPyl
AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
the enzyme attaches attaches L-pyrrolysine only to tRNA transcripts with a 3'-OH group at A76, whereas no aminoacylation at the 2'-OH group is detected
-
-
?
additional information
?
-
unlike most aminoacyl-tRNA synthetases, PylRS displays high substrate side chain promiscuity, low selectivity toward its substrate alpha-amine, and low selectivity toward the anticodon of tRNAPyl, overview. PylRS shows low selectivity toward the tRNA anticodon and low selectivity toward the Pyl alpha-amine
-
-
?
additional information
?
-
the archaeal tRNAPyl features a secondary structure that significantly diverges from that of canonical tRNAs
-
-
?
additional information
?
-
the recombinant pylS gene product charges tRNAPyl with Pyl, but the recombinant pylS gene product also succeeds in ligating [14C]Lys to tRNA. A mRNA secondary structure is definitely not necessary for the incorporation of Pyl at an amber codon. The binding of the side chain pyrroline of Pyl to the PylRS active site involves essentially van der Waals interactions. Replacing the side chain pyrroline with a similar size chemical component with a hydrophobic nature might retain the PylRS activity to aminoacylate tRNAPyl. PylRS weakly recognizes three non-canonical amino acids and mediates their incorporation into proteins at an amber codon in coordination with tRNAPyl, allowing the synthesis of proteins with site-specific lysine propionylation, butylation, and crotonylation
-
-
?
additional information
?
-
-
Methanosarcina cells have two pathways for acylating the suppressor tRNAPyl to ensure efficient translation of the in-frame UAG codon in case of pyrrolysine deficiency and safeguard the biosynthesis of the proteins whose genes contain this special codon, L-pyrrolysine is found in the Methanosarcina barkeri monomethylamine methyltransferase protein in a position that is encoded by an in-frame UAG stop codon in the mRNA, overview
-
-
?
additional information
?
-
-
pyrrolysine is required in e.g. methylamine methyltransferase MtmB, overview
-
-
?
additional information
?
-
-
while pyrrolysine is the natural substrate of PylRS, lysine is not recognized by the enzyme
-
-
?
additional information
?
-
-
structure of endogenous tRNAPyl, overview
-
-
?
additional information
?
-
-
synthetic L-pyrrolysine is attached as a free molecule to tRNACUA by PylS, an archaeal class II aminoacyl-tRNA synthetase, inability of recombinant PylS-His6 to synthesize lysyltRNACUA
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-pyrrolysine + tRNAPyl
AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
-
-
?
ATP + L-pyrrolysine + tRNAPyl
AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
-
-
-
?
ATP + L-pyrrolysine + tRNAPyl
AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
-
-
?
ATP + L-pyrrolysine + tRNAPyl
AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
direct charging of tRNA(CUA) with pyrrolysine in vitro and in vivo
-
-
?
ATP + L-pyrrolysine + tRNAPyl
AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
Pyl-tRNAPyl insertion at UAG, a specialized mRNA motif is not essential for stopcodon recoding, unlike for selenocysteine incorporation
-
-
?
ATP + L-pyrrolysine + tRNAPyl
AMP + diphosphate + L-pyrrolysyl-tRNAPyl
-
the enzyme attaches attaches L-pyrrolysine only to tRNA transcripts with a 3'-OH group at A76, whereas no aminoacylation at the 2'-OH group is detected
-
-
?
additional information
?
-
unlike most aminoacyl-tRNA synthetases, PylRS displays high substrate side chain promiscuity, low selectivity toward its substrate alpha-amine, and low selectivity toward the anticodon of tRNAPyl, overview. PylRS shows low selectivity toward the tRNA anticodon and low selectivity toward the Pyl alpha-amine
-
-
?
additional information
?
-
-
Methanosarcina cells have two pathways for acylating the suppressor tRNAPyl to ensure efficient translation of the in-frame UAG codon in case of pyrrolysine deficiency and safeguard the biosynthesis of the proteins whose genes contain this special codon, L-pyrrolysine is found in the Methanosarcina barkeri monomethylamine methyltransferase protein in a position that is encoded by an in-frame UAG stop codon in the mRNA, overview
-
-
?
additional information
?
-
-
pyrrolysine is required in e.g. methylamine methyltransferase MtmB, overview
-
-
?
additional information
?
-
-
while pyrrolysine is the natural substrate of PylRS, lysine is not recognized by the enzyme
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.39
2-amino-6-((R)-tetrahydrofuran-2-carboxamido)hexanoic acid
-
pH 7.2, 37°C
0.67
N-epsilon-cyclopentyloxycarbonyl-L-lysine
-
pH 7.2, 37°C, recombinant enzyme
0.00015 - 0.00098
additional information
-
equilibrium binding analysis, dissociation constants of the enzyme with tRNAPyl from different species, overview
-
0.044
L-pyrrolysine
wild type enzyme, at 37°C in 50 mM KCl, 10 mM MgCl2, 5 mM ATP, and 5 mM dithiothreitol in 10 mM HEPES buffer, pH 7.2
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.062
2-amino-6-((R)-tetrahydrofuran-2-carboxamido)hexanoic acid
-
pH 7.2, 37°C
0.1
L-pyrrolysine
wild type enzyme, at 37°C in 50 mM KCl, 10 mM MgCl2, 5 mM ATP, and 5 mM dithiothreitol in 10 mM HEPES buffer, pH 7.2
0.325
L-pyrrolysine
wild type enzyme, at 37°C in 50 mM KCl, 10 mM MgCl2, 5 mM ATP, and 5 mM dithiothreitol in 10 mM HEPES buffer, pH 7.2
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.16
2-amino-6-((R)-tetrahydrofuran-2-carboxamido)hexanoic acid
-
pH 7.2, 37°C
0.0071
2-amino-6-(cyclopentanecarboxamido)hexanoic acid
-
pH 7.2, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
sequence alignment indicated that full-length PylRS contains a C-terminal class II AARS catalytic core and an N-terminal domain that apparently does not share sequence homology with any structurally known protein domains. The three dimensional organization of the PylRS catalytic core resembles that of other synthetases from the Class II AARS family
physiological function
the genetic incorporation of the 22nd proteinogenic amino acid, pyrolysine (Pyl) at amber codon is achieved by the action of pyrrolysyl-tRNA synthetase (PylRS) together with its cognate tRNAPyl. When D-ornithine is provided in the growth medium, the clustered genes of pylT, pylS, pylC, and pylD were able to mediate amber suppression, pylC and pylD gene products are able to synthesize desmethyl-Pyl from D-ornithine and lysine and that PylRS tolerates alternative substrates
additional information
along with its special CUA anticodon for the recognition of amber codon, the pylT transcript, tRNAPyl, has a distinct anticodon stem of six base pairs instead of five base pairs as observed in most tRNAs, a single base between D and anticodon stems, a single base between D and acceptor stems, and a three-base small variable arm
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
the PylRS catalytic core resembles that of other synthetases from the Class II AARS family. It has a typical beta-sheet core surrounded by several helices, forming a Rossmann fold for the binding of ATP. Like most other class II aminoacyl-tRNA synthetases, PylRS also forms an obligate dimer. Each subunit has an active site
additional information
-
the PylRS sequence can be subdivided into three regions: the highly conserved class II aaRS catalytic core domain at the carboxy-terminal, the unique amino-terminal domain, and a highly variable region linking these two domains, residues from the PylRS amino-terminal domain affect activity in vivo
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
efforts to crystalize full-length PylRS are not successful due to the low solubility of the protein. The N-terminal domain is highly insoluble and aggregates full-length PylRS. But using the truncated C-terminal catalytic core of PylRS from Methanosarcina mazei, apo-PylRS and PylRS complexes with different ligands are successfully determined
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Y349F
the pyrrolysyl-tRNA synthetase/tRNAPyl pair is the most versatile and widespread system for the incorporation of non-canonical amino acids (ncAAs) into proteins in mammalian cells. Low yields of ncAA incorporation severely limit its applicability to relevant biological targets. Generation of two tRNAPyl variants that significantly boost the performance of the pyrrolysine system. Compared to the original tRNAPyl, the engineered tRNAs feature a canonical hinge between D- and T-loop, show higher intracellular concentrations and bear partially distinct post-transcriptional modifications. They allow efficient ncAA incorporation into a G-protein coupled receptor (GPCR) and simultaneous ncAA incorporation at two GPCR sites. Different combinations of recognition motifs for PylRS are introduced into Bos taurus mt-tRNASerCUA. Bicistronic plasmids are generated combining each tRNA with the PylRS from Methanosarcina barkeri, which bears the mutation Y349F for enhanced activity (PylRSF). In the presence of the PylRS substrate Lys(Boc), four tRNAs in the M series and five in the C series yield higher amber suppression compared to the tRNAPyl, whereas the other tRNAs show either lower efficiency or no amber suppression at all, overview
D2A
-
site-directed mutagenesis, the mutant shows 95% reduced activity compared to the wild-type enzyme
D2A/K4A
-
site-directed mutagenesis, the mutant shows almost completely reduced activity compared to the wild-type enzyme
D7A
-
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
G21L
-
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
H24A
-
site-directed mutagenesis, the mutant shows 95% reduced activity compared to the wild-type enzyme
I26G
-
site-directed mutagenesis, the mutant shows 80% reduced activity compared to the wild-type enzyme
K3A
-
site-directed mutagenesis, the mutant shows 80% reduced activity compared to the wild-type enzyme
K4A
-
site-directed mutagenesis, the mutant shows 95% reduced activity compared to the wild-type enzyme
R19A
-
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
S11A
-
site-directed mutagenesis, the mutant shows 95% reduced activity compared to the wild-type enzyme
S11A/T13A
-
site-directed mutagenesis, the mutant shows almost completely reduced activity compared to the wild-type enzyme
S18A
-
site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
T13A
-
site-directed mutagenesis, the mutant shows 95% reduced activity compared to the wild-type enzyme
W16A
-
site-directed mutagenesis, the mutant shows 35% reduced activity compared to the wild-type enzyme
additional information
additional information
-
truncation of the N-terminal region of PylS (DELTA92PylS) eliminates detectable tRNAPyl binding, but not catalytic activity
additional information
truncation of the N-terminal region of PylS (DELTA92PylS) eliminates detectable tRNAPyl binding, but not catalytic activity
additional information
engineering of mutants that display higher activities for their genetic incorporation than the wild-type PylRS and increased specificities, overview
additional information
-
construction of several truncation mutants, which show 90-99% reduced activity compared to the wild-type enzyme, overview
additional information
-
the genetic code of Escherichia coli can be expanded to include UAG-directed pyrrolysine incorporation into proteins
additional information
-
variant pyrrolysyl-tRNA synthetase/tRNACUA Pyl pairs created in Escherichia coli can be used to expand the genetic code of Saccharomyces cerevisiae through a simple system, overview. Variant pyrrolysyl-tRNA synthetase/tRNACUA Pyl pairs are site-specifically incorporated into proteins in yeast
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli BL21(DE3)
-
recombinant His6-tagged PylS from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene pylS, encoded in the pyl gene cluster, DNA and amino acid sequence analysis, recombinant expression in Escherichia coli, the pyl gene cluster codes all necessary enzymes for the biosynthesis of Pyl from Escherichia coli metabolites
expression of variant pyrrolysyl-tRNA synthetase/tRNACUA Pyl pairs in Saccharomyces cerevisiae, tRNA mutant variants, overview
-
functional co-expression with tRNAPyl in Escherichia coli, the recombinant enzyme is active with substrate analogues N-epsilon-D-prolyl-L-lysine and N-epsilon-cyclopentyloxycarbonyl-L-lysine
-
gene pylS, expression as His6-tagged enzyme in Escherichia coli strain BL21 (DE3), addition of pyrrolysine to Escherichia coli cells expressing pylT, encoding tRNACUA, and pylS results in the translation of UAG in vivo as a sense codon, inability of PylS-His6 to synthesize lysyltRNACUA, co-expression with gene mtmB1
-
gene pylS, expression of His-tagged wild-type and mutant enzymes in Escherichia coli BL21(DE3)
-
gene pylS, expression of operon pylTSBCD in Escherichia coli strain BL21 Tuner(DE3)
-
gene pylS, expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
molecular biology
PylRS as aminoacyl-tRNA synthetase allows the Pyl incorporation machinery to be easily engineered for the genetic incorporation of more than 100 non-canonical amino acids (NCAAs) or alpha-hydroxy acids into proteins at amber codon and the reassignment of other codons such as ochre UAA, opal UGA, and four-base AGGA codons to code NCAAs
synthesis
-
synthesis and genetic incorporation of aliphatic azides and alkynes into proteins using the natural pyrrolysyl tRNA synthetase/tRNACUA pair and the efficient bio-orthogonal labeling of these amino acids using [3+2] cycloaddition, i.e. click chemistry. Escherichia coli transformed with pBKPylS10 encoding pyrrolysyl tRNA synthetase and pMyo4TAGPylT-his610 encoding tRNACUA and a C-terminally hexahistidine tagged myoglobin gene with an amber codon at position 4 incorporates (2S)-2-amino-6-[[(prop-2-yn-1-yloxy)carbonyl]amino]hexanoic acid. The yield of protein containing (2S)-2-amino-6-[[(prop-2-yn-1-yloxy)carbonyl]amino]hexanoic acid is not improved by efforts to evolve the enzyme but is increased 5fold by increasing the concentration of (2S)-2-amino-6-[[(prop-2-yn-1-yloxy)carbonyl]amino]hexanoic acid 7.5fold
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Polycarpo, C.R.; Herring, S.; Berube, A.; Wood, J.L.; Soll, D.; Ambrogelly, A.
Pyrrolysine analogues as substrates for pyrrolysyl-tRNA synthetase
FEBS Lett.
580
6695-6700
2006
Methanosarcina barkeri
Herring, S.; Ambrogelly, A.; Gundllapalli, S.; O'Donoghue, P.; Polycarpo, C.R.; Soll, D.
The amino-terminal domain of pyrrolysyl-tRNA synthetase is dispensable in vitro but required for in vivo activity
FEBS Lett.
581
3197-3203
2007
Desulfitobacterium hafniense, Methanosarcina barkeri, Methanosarcina thermophila (Q1L6A3)
Blight, S.K.; Larue, R.C.; Mahapatra, A.; Longstaff, D.G.; Chang, E.; Zhao, G.; Kang, P.T.; Green-Church, K.B.; Chan, M.K.; Krzycki, J.A.
Direct charging of tRNA(CUA) with pyrrolysine in vitro and in vivo
Nature
431
333-335
2004
Methanosarcina barkeri
Polycarpo, C.; Ambrogelly, A.; Berube, A.; Winbush, S.M.; McCloskey, J.A.; Crain, P.F.; Wood, J.L.; Soll, D.
An aminoacyl-tRNA synthetase that specifically activates pyrrolysine
Proc. Natl. Acad. Sci. USA
101
12450-12454
2004
Methanosarcina barkeri, Methanosarcina barkeri Fusaro / DSM 804
Nguyen, D.P.; Lusic, H.; Neumann, H.; Kapadnis, P.B.; Deiters, A.; Chin, J.W.
Genetic encoding and labeling of aliphatic azides and alkynes in recombinant proteins via a pyrrolysyl-tRNA Synthetase/tRNA(CUA) pair and click chemistry
J. Am. Chem. Soc.
131
8720-8721
2009
Methanosarcina barkeri
Hancock, S.M.; Uprety, R.; Deiters, A.; Chin, J.W.
Expanding the genetic code of yeast for incorporation of diverse unnatural amino acids via a pyrrolysyl-tRNA synthetase/tRNA pair
J. Am. Chem. Soc.
132
14819-14824
2010
Methanosarcina barkeri
Gaston, M.A.; Zhang, L.; Green-Church, K.B.; Krzycki, J.A.
The complete biosynthesis of the genetically encoded amino acid pyrrolysine from lysine
Nature
471
647-650
2011
Methanosarcina barkeri
Englert, M.; Moses, S.; Hohn, M.; Ling, J.; ODonoghue, P.; Soell, D.
Aminoacylation of tRNA 2'- or 3'-hydroxyl by phosphoseryl- and pyrrolysyl-tRNA synthetases
FEBS Lett.
587
3360-3364
2013
Desulfitobacterium hafniense, Methanosarcina barkeri
Jiang, R.; Krzycki, J.A.
PylSn and the homologous N-terminal domain of pyrrolysyl-tRNA synthetase bind the tRNA that is essential for the genetic encoding of pyrrolysine
J. Biol. Chem.
287
32738-32746
2012
Desulfitobacterium hafniense, Methanosarcina barkeri, Methanosarcina barkeri (Q6WRH6)
Li, W.T.; Mahapatra, A.; Longstaff, D.G.; Bechtel, J.; Zhao, G.; Kang, P.T.; Chan, M.K.; Krzycki, J.A.
Specificity of pyrrolysyl-tRNA synthetase for pyrrolysine and pyrrolysine analogs.
J. Mol. Biol.
385
1156-1164
2009
Methanosarcina barkeri
Wan, W.; Tharp, J.M.; Liu, W.R.
Pyrrolysyl-tRNA synthetase an ordinary enzyme but an outstanding genetic code expansion tool
Biochim. Biophys. Acta
1844
1059-1070
2014
Methanosarcina barkeri (Q6WRH6), Methanosarcina mazei (Q8PWY1), Methanosarcina mazei ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88 (Q8PWY1)
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