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Information on EC 6.1.1.16 - cysteine-tRNA ligase and Organism(s) Escherichia coli and UniProt Accession P21888
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6.1.1.16 cysteine-tRNA ligaseSpecify your search results
Word Map
- 6.1.1.16
- synthetases
- aminoacyl-trnas
- aminoacylation
-
cys-trnacys
-
prolyl-trna
- prors
- seprs
-
cysteinyl-trnacys
- asnrs
-
atp-ppi
- ilers
- valrs
-
o-phosphoseryl-trna
- maripaludis
-
aarss
-
sep-trna:cys-trna
- sepcyss
- o-phosphoserine
- drug development
- molecular biology
- medicine
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
cysteinyl-trna synthetase, cysrs, cars2, cars1, cysteinyl trna synthetase, class i cysrs, class i cysteinyl-trna synthetase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CysRS
Cysteine translase
Cysteine--tRNA ligase
Cysteinyl-transfer ribonucleate synthetase
Cysteinyl-transfer RNA synthetase
Cysteinyl-tRNA synthetase
Synthetase, cysteinyl-transfer ribonucleate
CysRS
-
-
-
-
Cysteine translase
-
-
-
-
Cysteine--tRNA ligase
-
-
-
-
Cysteinyl-transfer ribonucleate synthetase
-
-
-
-
Cysteinyl-transfer RNA synthetase
-
-
-
-
Cysteinyl-tRNA synthetase
-
-
-
-
Synthetase, cysteinyl-transfer ribonucleate
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-cysteine + tRNACys = AMP + diphosphate + L-cysteinyl-tRNACys
substrate binding mechanism, induced fit
ATP + L-cysteine + tRNACys = AMP + diphosphate + L-cysteinyl-tRNACys
the class I tRNA synthetase CysRS is rate-limited by release of aminoacyl-tRNA, class I synthetases share two signature motifs, HIGH and KMSKS, and build their active site by the ubiquitous Rossmann nucleotide-binding fold, the tight aminoacyl-tRNA product binding by class I enzymes correlates with the ability of EF-Tu to form a ternary complex with class I but not class II synthetases, and the further capacity of this protein to enhance the rate of aminoacylation by class I synthetases
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
esterification
Aminoacylation
esterification
-
-
-
-
Aminoacylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-cysteine:tRNACys ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY
37318-56-2
-
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 + L-cysteine + tRNACys mutant
AMP + diphosphate + L-cysteinyl-tRNACys mutant
-
tRNA substrate is a tRNACys with mutation at the core tertiary Levitt pair from wild-type G15.C48 to mutant G15.G48, leading to a higher activity
-
?
ATP + L-cysteine + tRNACysA36G
AMP + diphosphate + L-cysteinyl-tRNACysA36G
-
relative activity compared to wild-type tRNACys as a substrate: 0.01
-
-
?
ATP + L-cysteine + tRNACysC35U
AMP + diphosphate + L-cysteinyl-tRNACysC35U
-
relative activity compared to wild-type tRNACys as a substrate: 0.005
-
-
?
ATP + L-cysteine + tRNACysG15C/C48G
AMP + diphosphate + L-cysteinyl-tRNACysG15C/C48G
-
relative activity compared to wild-type tRNACys as a substrate: 0.03
-
-
?
ATP + L-cysteine + tRNACysG34C
AMP + diphosphate + L-cysteinyl-tRNACysG34C
-
relative activity compared to wild-type tRNACys as a substrate: 0.001
-
-
?
ATP + L-cysteine + tRNACysU73G
AMP + diphosphate + L-cysteinyl-tRNACysU73G
-
relative activity compared to wild-type tRNACys as a substrate: 0.00002
-
-
?
ATP + L-cysteine + tRNAGln duoble-mutant
AMP + diphosphate + L-cysteinyl-tRNAGln double-mutant
-
tRNA substrate is a tRNAGln with introduced tRNACys indentitiy nucleotides at the acceptor and anticodon ends and a core tertiary Levitt pair equivalent to tRNAGln of G15.G48, poor activity
-
?
ATP + L-cysteine + tRNAGln mutant
AMP + diphosphate + L-cysteinyl-tRNAGln mutant
-
tRNA substrate is a tRNAGln with introduced tRNACys indentitiy nucleotides at the acceptor and anticodon ends and a core tertiary Levitt pair equivalent to tRNACys of G15.C48
-
?
L-Cysteinyl-tRNACys
Cysteine thiolactone + ?
-
deacylation in which nucleophilic sulfur of the side chain of cysteine in Cys-tRNACys attacks its carboxyl carbon, synthesis of Cys-tRNACys and cyclization of cysteine to thiolactone occur in a single active site
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
enzyme is highly specific for L-cysteine and does not possess the editing activity characteristic for other tRNA synthetases
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
the enzyme is rate-limited by release of aminoacyl-tRNA
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
tRNACys mutants: greatest loss of activity caused by mutation of a single nucleotide, occurs when the discriminator U73 is changed, mutations in the wobble nucleotide of the anticodon also cause reductions in the specificity constant of 3 orders of magnitude, while mutations in the other anticodon nucleotides causes lesser effects
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
enzyme is highly specific for L-cysteine without performing an editing reaction, tightly bound zinc is the primary determinant of selectivity against non-cognate amino acids
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
the attachment of cysteine to tRNACys by the class I cysteinyl-tRNA synthetase is flexible. The enzyme is capable of using either the 2' or 3'-hydroxyl group as the attachment site
-
-
?
additional information
?
-
-
selenocysteine can replace cysteine in ATP-diphosphate exchange
-
-
?
additional information
?
-
-
alanine shows minor activity in ATP-diphosphate exchange
-
-
?
additional information
?
-
-
2-aminobutyric acid can replace cysteine in ATP-diphosphate exchange
-
-
?
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-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
1 ion bound at the base of the active site cleft, important for tRNA substrate specificity, single direct interaction with cysteine thiolate substrate
Zn2+
-
can be substituted by Co2+, tightly bound, 1 ion per enzyme molecule, bound at the base of the active site cleft, primary determinant of selectivity against non-cognate amino acids
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00047
L-cysteine
mutant enzyme M294A, pH and temperature not specified in the publication
0.00052
L-cysteine
mutant enzyme E354Q, pH and temperature not specified in the publication
0.00055
L-cysteine
mutant enzyme H297A, pH and temperature not specified in the publication
0.00066
L-cysteine
mutant enzyme M294A/H297A, pH and temperature not specified in the publication
0.0012
L-cysteine
wild type enzyme, pH and temperature not specified in the publication
0.0018
L-cysteine
mutant enzyme R42A, pH and temperature not specified in the publication
0.002
L-cysteine
mutant enzyme H40A, pH and temperature not specified in the publication
0.0075
L-cysteine
mutant enzyme R427A, pH and temperature not specified in the publication
0.0076
L-cysteine
mutant enzyme M294A/R427A, pH and temperature not specified in the publication
0.01
L-cysteine
mutant enzyme E354Q/R427A, pH and temperature not specified in the publication
2.4
L-cysteine
mutant enzyme H40A/R42A, pH and temperature not specified in the publication
0.22
ATP
-
ATP-diphosphate exchange reaction, recombinant His-tagged Co2+-wild-type enzyme
0.25
ATP
-
ATP-diphosphate exchange reaction, recombinant His-tagged Zn2+-wild-type enzyme
0.29
ATP
-
ATP-diphosphate exchange reaction, recombinant Zn2+-wild-type enzyme
0.77
ATP
-
ATP-diphosphate exchange reaction, recombinant W205Y mutant enzyme
0.022
L-cysteine
-
ATP-diphosphate exchange reaction, recombinant Zn2+-wild-type enzyme
0.029
L-cysteine
-
ATP-diphosphate exchange reaction, recombinant His-tagged Co2+-wild-type enzyme
0.031
L-cysteine
-
ATP-diphosphate exchange reaction, recombinant His-tagged Zn2+-wild-type enzyme
3.61
L-cysteine
-
ATP-diphosphate exchange reaction, recombinant W205Y mutant enzyme
0.00035
tRNACys
-
aminoacylation reaction, recombinant Zn2+-wild-type enzyme
0.0004
tRNACys
-
aminoacylation reaction, recombinant His-tagged Co2+-wild-type enzyme
0.0012
tRNACys
-
aminoacylation reaction, recombinant His-tagged Zn2+-wild-type enzyme
0.095
tRNACys
-
aminoacylation reaction, recombinant C28S/C209S mutant enzyme
additional information
additional information
thermodynamics, single turnover and burst kinetics of CysRS, steady-state and transient kinetic analyses of class I CysRS, the enzyme is rate-limited by release of aminoacyl-tRNA, recombinant His-tagged enzyme, overview
-
additional information
additional information
-
Km-values of mutant tRNA molecules
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001
L-cysteine
mutant enzyme H40A/R42A, pH and temperature not specified in the publication
0.0093
L-cysteine
mutant enzyme H40A, pH and temperature not specified in the publication
0.02
L-cysteine
mutant enzyme M294A/R427A, pH and temperature not specified in the publication
0.027
L-cysteine
mutant enzyme R427A, pH and temperature not specified in the publication
0.082
L-cysteine
mutant enzyme E354Q, pH and temperature not specified in the publication
0.088
L-cysteine
mutant enzyme M294A/H297A, pH and temperature not specified in the publication
0.14
L-cysteine
mutant enzyme M294A, pH and temperature not specified in the publication
0.16
L-cysteine
mutant enzyme H297A, pH and temperature not specified in the publication
0.49
L-cysteine
mutant enzyme E354Q/R427A, pH and temperature not specified in the publication
1.1
L-cysteine
mutant enzyme R42A, pH and temperature not specified in the publication
1.2
L-cysteine
wild type enzyme, pH and temperature not specified in the publication
0.3
ATP
-
ATP-diphosphate exchange reaction, recombinant W205Y mutant enzyme
57
ATP
-
ATP-diphosphate exchange reaction, recombinant His-tagged Co2+-wild-type enzyme
91
ATP
-
ATP-diphosphate exchange reaction, recombinant Zn2+-wild-type enzyme
142
ATP
-
ATP-diphosphate exchange reaction, recombinant His-tagged Zn2+-wild-type enzyme
0.28
L-cysteine
-
ATP-diphosphate exchange reaction, recombinant W205Y mutant enzyme
35
L-cysteine
-
ATP-diphosphate exchange reaction, recombinant His-tagged Co2+-wild-type enzyme
79
L-cysteine
-
ATP-diphosphate exchange reaction, recombinant Zn2+-wild-type enzyme
100
L-cysteine
-
ATP-diphosphate exchange reaction, recombinant His-tagged Zn2+-wild-type enzyme
0.005
tRNACys
-
aminoacylation reaction, recombinant C28S/C209S mutant enzyme
0.5
tRNACys
-
aminoacylation reaction, recombinant His-tagged Co2+-wild-type enzyme
2.5
tRNACys
-
aminoacylation reaction, recombinant His-tagged Zn2+-wild-type enzyme
additional information
additional information
-
turnover numbers of mutant tRNA molecules
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3
L-cysteine
mutant enzyme M294A/R427A, pH and temperature not specified in the publication
3.8
L-cysteine
mutant enzyme R427A, pH and temperature not specified in the publication
5.3
L-cysteine
mutant enzyme H40A/R42A, pH and temperature not specified in the publication
5.4
L-cysteine
mutant enzyme H40A, pH and temperature not specified in the publication
50
L-cysteine
mutant enzyme E354Q/R427A, pH and temperature not specified in the publication
140
L-cysteine
mutant enzyme M294A/H297A, pH and temperature not specified in the publication
160
L-cysteine
mutant enzyme E354Q, pH and temperature not specified in the publication
300
L-cysteine
mutant enzyme M294A, pH and temperature not specified in the publication
320
L-cysteine
mutant enzyme H297A, pH and temperature not specified in the publication
750
L-cysteine
mutant enzyme R42A, pH and temperature not specified in the publication
1000
L-cysteine
wild type enzyme, pH and temperature not specified in the publication
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
-
although the nucleotides in tRNA required for aminoacylation are conserved in evolution, bacterial aminoacyl-transfer RNA synthetases are unable to acylate eukaryote-specific tRNA. Whereas Escherichia coli CysRS cannot acylate human tRNACys, the fusion of a eukaryote-specific domain of human CysRS overcomes the cross-species barrier in human tRNACys. In addition to enabling recognition of the sequence differences in the tertiary core of tRNACys, the fused eukaryotic domain redirects the specificity of Escherichia coli CysRS from the A37 present in bacterial tRNACys to the G37 in mammals. The accuracy of codon recognition on the ribosome is also highly sensitive to the A37G transition in tRNACys
metabolism
-
the enzyme plays a crucial role in endogenous cysteine hydropersulfide production and serves as the principal cysteine persulfide synthase in vivo
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
the enzyme forms a class I ternary complex with EF-Tu, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, crystals of enzyme bound to tRNACys at a resolution of 2.3 A
purified recombinant free enzyme or cysteine and ATP complexed enzyme, hanging-drop vapour diffusion method, 17°C, 0.001 ml protein solution: 6 mg/ml enzyme, 10 mM HEPES, pH 7.4, 50 mM NaCl, 1 mM DTT, 5 mM MgCl2, 5 mM ATP, 10 mM cysteine, plus equal volume of reservoir solution: 0.1 M sodium cacodylate, pH 6.5, 15-17% PEG 8000, 0.2 M magnesium acetate, 2% tert-butanol, 1-3 weeks, cysteine but not ATP is required for crystal growth, X-ray diffraction structure determination at 2.3-3.0 A resolution, and analysis
purified enzyme complexed with ATP and cysteine, hanging-drop vapour diffusion from ammonium sulfate precipitant containing solution, X-ray diffraction structure analysis at 2.7 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E354Q
the mutant has decreased kcat and Km values leading to an overall decrease in kcat/Km by 6.8fold relative to the wild type enzyme
E354Q/R427A
the mutant has a decreased kcat and an increased Km leading to an overall decrease in kcat/Km by 22fold relative to the wild type enzyme
H297A
the mutant has a decreased kcat and Km values leading to an overall decrease in kcat/Km by 3.4fold relative to the wild type enzyme
H404A/R42A
the mutant has a decreased kcat and an increased Km leading to an overall decrease in kcat/Km by 209fold relative to the wild type enzyme
H40A
the mutant has a decreased kcat and an increased Km leading to an overall decrease in kcat/Km by 204fold relative to the wild type enzyme
M294A
the mutant has decreased kcat and Km values leading to an overall decrease in kcat/Km by 3.7fold relative to the wild type enzyme
M294A/H297A
the mutant has a decreased kcat and Km values leading to an overall decrease in kcat/Km by 8.1fold relative to the wild type enzyme
M294A/R427A
the mutant has a decreased kcat and an increased Km leading to an overall decrease in kcat/Km by 370fold relative to the wild type enzyme
R427A
the mutant has a decreased kcat and an increased Km leading to an overall decrease in kcat/Km by 291fold relative to the wild type enzyme
R42A
the mutant has a decreased kcat and an increased Km leading to an overall decrease in kcat/Km by 1.5fold relative to the wild type enzyme
C209S
-
the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.0031% of the wild-type ratio
C28S
-
the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.012% of the wild-type ratio
C28S/C209S
C28S/C209S/H234N/E238Q
C36S/C214S/C244S
-
site-directed mutagenesis, activity is similar to the wild-type enzyme, but the affinity for cysteine binding is increased
DELTA288-461
-
the ratio of turnover number to Km-value for ATP in ATP-diphosphate exchange is 7% of the wild-type ratio
DELTA328-461
-
the ratio of turnover number to Km-value for ATP in ATP-diphosphate exchange is 0.32% of the wild-type ratio, aminoacylation of tRNACys is not detectable
E354Q
-
the ratio of turnover number to Km-value of aminoacylation of tRNACys is 10% of the wild-type ratio
H206S
-
the ratio of turnover number to Km-value of aminoacylation of tRNACys is 60% of the wild-type ratio
H224N/H235N
-
the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.042% of the wild-type ratio
H224S
-
the ratio of turnover number to Km-value of aminoacylation of tRNACys is 5.7% of the wild-type ratio
H234N/E238Q
-
the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.0059% of the wild-type ratio
H234S
-
the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.015% of the wild-type ratio
H235S
-
the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.38% of the wild-type ratio
H238S
-
the ratio of turnover number to Km-value of aminoacylation of tRNACys is 30% of the wild-type ratio
H256S
-
the ratio of turnover number to Km-value of aminoacylation of tRNACys is 10% of the wild-type ratio
N351D
-
the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.25% of the wild-type ratio
V27E
-
mutation does not affect the discrimination of the enzyme for serine. 4fold increase in Km-value for cysteine and 9fold reduction of turnover number for ATP
W205F
-
the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.55% of the wild-type ratio
W205Y
-
site-directed mutagenesis, highly reduced activity, highly increased Km for cysteine
additional information
C28S/C209S
-
site-directed mutagenesis, no ATP-diphosphate exchange activity, residual aminoacylation activity
C28S/C209S
-
the ratio of turnover number to Km-value of aminoacylation of tRNACys is 0.0026% of the wild-type ratio
C28S/C209S/H234N/E238Q
-
site-directed mutagensis, mutation of all zinc binding ligands, complete loss of bound zinc, weak ability to bind serine, thus loss of amino acid substrate discrimination ability
additional information
-
construction of a Co2+-substituted wild-type enzyme, similar properties as the Zn2+-wild-type enzyme but slightly reduced activity
additional information
-
construction of a fusion of a eukaryote-specific domain of human CysRS enabling recognition of the sequence differences in the tertiary core of tRNACys. The fused eukaryotic domain redirects the specificity of Escherichia coli CysRS from the A37 present in bacterial tRNACys to the G37 in mammals
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Eriani, G.; Dirheimer, G.; Gangloff, J.
Cysteinyl-tRNA synthetase: determination of the last E. coli aminoacyl-tRNA synthetase primary structure
Nucleic Acids Res.
19
265-269
1991
Escherichia coli
Jakubowski, H.
Editing function of Escherichia coli cysteinyl-tRNA synthetase: cyclization of cysteine to cysteine thiolactone
Nucleic Acids Res.
22
1155-1160
1994
Escherichia coli
Komatsoulis, G.A.; Abelson, J.
Recognition of tRNACys by Escherichia coli cysteinyl-tRNA synthetase [published erratum appears in Biochemistry 1993 Dec 7;32(48):13374]
Biochemistry
32
7435-7444
1993
Escherichia coli
Bohman, K.; Isaksson, L.A.
Temperature-sensitive mutants in cysteinyl-tRNA ligase of E. coli K-12
Mol. Gen. Genet.
176
53-55
1979
Escherichia coli
Fersht, A.R.; Dingwall, C.
Cysteinyl-tRNA synthetase from Escherichia coli does not need an editing mechanism to reject serine and alanine. High binding energy of small groups in specific molecular interactions
Biochemistry
18
1245-1249
1979
Escherichia coli
McCorquodale, D.J.
The separation and partial purification of aminoacyl-RNA synthetases from Escherichia coli
Biochim. Biophys. Acta
91
541-548
1964
Escherichia coli
Newberry, K.J.; Kohn, J.; Hou, Y.M.; Perona, J.J.
Crystallization and preliminary diffraction analysis of Escherichia coli cysteinyl-tRNA synthetase
Acta Crystallogr. Sect. D
55
1046-1047
1999
Escherichia coli
Newberry, K.J.; Hou, Y.M.; Perona, J.J.
Structural origins of amino acid selection without editing by cysteinyl-tRNA synthetase
EMBO J.
21
2778-2787
2002
Escherichia coli (P21888), Escherichia coli
Sherlin, L.D.; Bullock, T.L.; Newberry, K.J.; Lipman, R.S.; Hou, Y.M.; Beijer, B.; Sproat, B.S.; Perona, J.J.
Influence of transfer RNA tertiary structure on aminoacylation efficiency by glutaminyl and cysteinyl-tRNA synthetases
J. Mol. Biol.
299
431-446
2000
Escherichia coli
Zhang, C.M.; Christian, T.; Newberry, K.J.; Perona, J.J.; Hou, Y.M.
Zinc-mediated amino acid discrimination in cysteinyl-tRNA synthetase
J. Mol. Biol.
327
911-917
2003
Escherichia coli
Zhang, C.M.; Hou, Y.M.
Domain-domain communication for tRNA aminoacylation: the importance of covalent connectivity
Biochemistry
44
7240-7249
2005
Escherichia coli
Ruan, B.; Nakano, H.; Tanaka, M.; Mills, J.A.; DeVito, J.A.; Min, B.; Low, K.B.; Battista, J.R.; Soll, D.
Cysteinyl-tRNA(Cys) formation in Methanocaldococcus jannaschii: the mechanism is still unknown
J. Bacteriol.
186
8-14
2004
Escherichia coli
Shitivelband, S.; Hou, Y.M.
Breaking the stereo barrier of amino acid attachment to tRNA by a single nucleotide
J. Mol. Biol.
348
513-521
2005
Escherichia coli
Hauenstein, S.; Zhang, C.M.; Hou, Y.M.; Perona, J.J.
Shape-selective RNA recognition by cysteinyl-tRNA synthetase
Nat. Struct. Mol. Biol.
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2004
Escherichia coli (P21888), Escherichia coli
Zhang, C.M.; Perona, J.J.; Ryu, K.; Francklyn, C.; Hou, Y.M.
Distinct kinetic mechanisms of the two classes of aminoacyl-tRNA synthetases
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2006
Escherichia coli (P21888)
Zhang, C.M.; Liu, C.; Slater, S.; Hou, Y.M.
Aminoacylation of tRNA with phosphoserine for synthesis of cysteinyl-tRNA(Cys)
Nat. Struct. Mol. Biol.
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2008
Escherichia coli
Liu, C.; Gamper, H.; Liu, H.; Cooperman, B.S.; Hou, Y.M.
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Nat. Commun.
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2011
Escherichia coli
Ghosh, A.; Sakaguchi, R.; Liu, C.; Vishveshwara, S.; Hou, Y.M.
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Escherichia coli (P21888)
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Escherichia coli, Homo sapiens, Mus musculus
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