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mature [tRNAIle2]-cytidine34 + L-lysine + ATP
mature [tRNAIle2]-2-lysylcytidine34 + AMP + diphosphate
TilS can modify both types of tRNA, pre-tRNAIle2 and mature tRNAIle2, with comparable efficiencies. TilS specifically recognizes the entire L-shape structure in pre-tRNAIle2 through extensive interactions coupled with sequential domain movements. TilS prevents the recognition of tRNAIle2 by methionyl-tRNA synthetase and achieves high specificity for its substrate
-
-
?
precursor [tRNAIle2]-cytidine34 + L-lysine + ATP
precursor [tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
TilS can modify both types of tRNA, pre-tRNAIle2 and mature tRNAIle2, with comparable efficiencies. TilS specifically recognizes the entire L-shape structure in pre-tRNAIle2 through extensive interactions coupled with sequential domain movements. TilS prevents the recognition of tRNAIle2 by methionyl-tRNA synthetase and achieves high specificity for its substrate
-
-
?
[tRNAIle2]-cytidine34 + L-isoleucine + ATP
[tRNAIle2]-2-L-isoleucylcytidine34 + AMP + diphosphate
the tRNAIle2(CAU) gene products are modified by TilS to produce tRNAIle2(LAU), while tRNAIle2(UAU) lacks modification especially in the anticodon sequence. tRNAIle2(LAU) is charged with isoleucine but tRNAIle2(UAU) is not
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + 7-deazaadenosine 5'-triphosphate
[tRNAIle2]-2-L-lysylcytidine34 + 7-deazaadenosine 5'-phosphate + diphosphate
Vmax/Km is 8.6% of Vmax/Km for ATP
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + 8-azidoadenosine 5'-triphosphate
[tRNAIle2]-2-L-lysylcytidine34 + 8-azidoadenosine 5'-phosphate + diphosphate
Vmax/Km is 2.3% of Vmax/Km for ATP
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-lysidine34 + AMP + diphosphate + H2O
[tRNAIle2]-cytidine34 + L-lysine + N6-methyladenosine-5'-triphosphate
[tRNAIle2]-2-L-lysylcytidine34 + N6-methyladenosine-5'-phosphate + diphosphate
Vmax/Km is 4.7% of Vmax/Km for ATP
-
-
?
additional information
?
-
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
-
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
-
-
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
C34 of tRNAIle2 is adenylated by an ATP lying across the central hole of the dinucleotide-binding fold domain. A lysine, which is activated at a loop appended to the dinucleotide-binding fold domain, nucleophilically attacks the C2 carbon from the rear
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
the enzyme generates lysidine at the wobble position of tRNAIle. The enzyme is essential for the decoding of AUA codons in the cell
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
lysidine synthesis TilS directly converts the amino acid specificity from methionine to isoleucine in vitro
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
-
-
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
-
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
-
-
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
bacteria decode the isoleucine codon AUA using a tRNA species that is posttranscriptionally modified at the wobble position of the anticodon with a lysine-containing cytidine derivative called lysidine. The lysidine modification of tRNAIle2 is an essential identity determinant for proper aminoacylation by isoleucyl tRNA synthetase and codon recognition on the ribosome. The ATP- and lysine-dependent formation of lysidine is catalyzed by tRNAIle-lysidine synthetase
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
-
enzyme catalyzes the lysylation of C34 (wobble position) in the precursor tRNAIle(CAU), thereby leading to the formation of tRNAIle(lysidineAU). The formation of lysidine by this essential enzyme allows recognition of tRNAIle(lysidineCAU) by Ile-tRNA synthetase and switches the base pairing of the tRNA from AUG (Met) to AUA (Ile)
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
-
the enzyme generates lysidine at the wobble position of tRNAIle. The enzyme is essential for the decoding of AUA codons in the cell
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
-
lysidine synthesis consists of two consecutive reactions that involve an adenylated tRNA intermediate. A mutation study reveals that Escherichia coli TilS discriminates tRNAIle from the structurally similar tRNAMet having the same anticodon loop by recognizing the anticodon loop, the anticodon stem, and the acceptor stem. TilS binds to the anticodon region and 3' side of the acceptor stem, which cover the recognition sites. A dedicated mechanism is embedded in tRNAIle that controls its recognition and discrimination by TilS
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
-
lysidine synthesis TilS directly converts the amino acid specificity from methionine to isoleucine in vitro
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
TilS specifically interacts with the isolated Escherichia coli tRNAIle2. Molecular mechanism of lysidine formation consists of two consecutive reactions involving the adenylated tRNA intermediate. TilS activates the C-2 position of C34 by forming an adenylate intermediate. Second, nucleophilic attack of the C-2 position of the intermediate by the epsilon-amino group of lysine completes the reaction
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
-
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
the tRNAIle2(CAU) gene products are modified by TilS to produce tRNAIle2(LAU), while tRNAIle2(UAU) lacks modification especially in the anticodon sequence. tRNAIle2(LAU) is charged with isoleucine but tRNAIle2(UAU) is not
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-lysidine34 + AMP + diphosphate + H2O
-
-
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-lysidine34 + AMP + diphosphate + H2O
-
-
-
-
?
additional information
?
-
no substrate: N1-methyladenosine-5'-triphosphate, 2-aminoadenosine-5'-triphosphate, 2-amino-6-chloropurineriboside-5'-triphosphate, and 6-chloropurineriboside-5'-triphosphate
-
-
?
additional information
?
-
-
no substrate: N1-methyladenosine-5'-triphosphate, 2-aminoadenosine-5'-triphosphate, 2-amino-6-chloropurineriboside-5'-triphosphate, and 6-chloropurineriboside-5'-triphosphate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-lysidine34 + AMP + diphosphate + H2O
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
-
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
the enzyme generates lysidine at the wobble position of tRNAIle. The enzyme is essential for the decoding of AUA codons in the cell
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
-
-
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
-
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
bacteria decode the isoleucine codon AUA using a tRNA species that is posttranscriptionally modified at the wobble position of the anticodon with a lysine-containing cytidine derivative called lysidine. The lysidine modification of tRNAIle2 is an essential identity determinant for proper aminoacylation by isoleucyl tRNA synthetase and codon recognition on the ribosome. The ATP- and lysine-dependent formation of lysidine is catalyzed by tRNAIle-lysidine synthetase
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
-
enzyme catalyzes the lysylation of C34 (wobble position) in the precursor tRNAIle(CAU), thereby leading to the formation of tRNAIle(lysidineAU). The formation of lysidine by this essential enzyme allows recognition of tRNAIle(lysidineCAU) by Ile-tRNA synthetase and switches the base pairing of the tRNA from AUG (Met) to AUA (Ile)
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
-
the enzyme generates lysidine at the wobble position of tRNAIle. The enzyme is essential for the decoding of AUA codons in the cell
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
-
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-lysidine34 + AMP + diphosphate + H2O
-
-
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-lysidine34 + AMP + diphosphate + H2O
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(5R)-5-hydroxy-L-lysine
-
3-bromo-N-(3-methoxyphenyl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine
4,5-trans-dehydro-L-lysine
-
4-(2-fluoro-5-methoxyanilino)-5,8-dihydropyrido[2,3-d]pyrimidin-7(6H)-one
8-azaadenosine 5-triphosphate
-
adenosine 5-O-(1-thiotriphosphate)
-
alpha,beta-methyleneadenosine 5'-triphosphate
-
benzimidazoleriboside 5-triphosphate
-
beta,gamma-methyleneadenosine 5'-triphosphate
-
mutated tRNAIle2
C34G-tRNAILe2
-
N-(3-methoxyphenyl)-5-methyl-7H-pyrrolo[2,3-d]pyrimidin-4-amine
N-acetylethylenediamine
-
N-alpha-methyl-L-lysine
-
3-bromo-N-(3-methoxyphenyl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine
-
competitive with respect to ATP
3-bromo-N-(3-methoxyphenyl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine
-
competitive with respect to ATP
4-(2-fluoro-5-methoxyanilino)-5,8-dihydropyrido[2,3-d]pyrimidin-7(6H)-one
-
competitive with respect to ATP
4-(2-fluoro-5-methoxyanilino)-5,8-dihydropyrido[2,3-d]pyrimidin-7(6H)-one
-
competitive with respect to ATP
N-(3-methoxyphenyl)-5-methyl-7H-pyrrolo[2,3-d]pyrimidin-4-amine
-
competitive with respect to ATP
N-(3-methoxyphenyl)-5-methyl-7H-pyrrolo[2,3-d]pyrimidin-4-amine
-
competitive with respect to ATP
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0.0018
7-deazaadenosine-5-triphosphate
pH 8.5, 21°C
0.01
8-azidoadenosine-5-triphosphate
pH 8.5, 21°C
0.00014
mature [tRNAIle2]-cytidine34
pH 7.8, 60°C
-
0.0217
N6-methyladenosine-5-triphosphate
pH 8.5, 21°C
0.00008
precursor [tRNAIle2]-cytidine34
pH 7.8, 60°C
-
0.00038 - 0.0202
[tRNAIle2]-cytidine34
additional information
additional information
-
kinetic parameters of Escherichia coli TilS with various tRNAIle2 mutants and with tRNAMet mutants
-
0.0016
ATP
pH 8.5, 21°C
0.0077
ATP
pH 7.8, 60°C, mutant enzyme H133A
0.019
ATP
pH 7.8, 60°C, wild-type enzyme
0.0385
ATP
pH 7.8, 60°C, mutant enzyme E106A
0.0412
ATP
pH 7.8, 60°C, mutant enzyme R174A
0.0412
ATP
pH 7.8, 60°C, mutant enzyme W188A
0.135
ATP
pH 7.8, 60°C, mutant enzyme E140A
0.155
ATP
pH 7.8, 60°C, mutant enzyme Y114A
0.255
ATP
pH 7.8, 60°C, mutant enzyme S37A
0.287
ATP
pH 7.8, 60°C, mutant enzyme R205A
0.38
L-lysine
-
pH 7.8, 37°C
0.629
L-lysine
pH 7.8, 60°C, wild-type enzyme
1.01
L-lysine
pH 7.8, 60°C, mutant enzyme R205A
1.04
L-lysine
pH 7.8, 60°C, mutant enzyme H133A
1.15
L-lysine
pH 7.8, 60°C, mutant enzyme R174A
1.3
L-lysine
pH 7.8, 60°C, mutant enzyme E106A
1.37
L-lysine
pH 7.8, 60°C, mutant enzyme E140A
3.05
L-lysine
pH 7.8, 60°C, mutant enzyme Y114A
0.00038
[tRNAIle2]-cytidine34
-
unmodified tRNAIle2, pH 7.8, 37°C
0.0019
[tRNAIle2]-cytidine34
pH 7.8, 60°C, mutant enzyme E106A
0.0033
[tRNAIle2]-cytidine34
pH 7.8, 60°C,wild-type enzyme
0.0035
[tRNAIle2]-cytidine34
pH 7.8, 60°C, mutant enzyme H133A
0.0074
[tRNAIle2]-cytidine34
pH 7.8, 60°C, mutant enzyme Y114A
0.0119
[tRNAIle2]-cytidine34
pH 7.8, 60°C, mutant enzyme R205A
0.0157
[tRNAIle2]-cytidine34
pH 7.8, 60°C, mutant enzyme E140A
0.0202
[tRNAIle2]-cytidine34
pH 7.8, 60°C, mutant enzyme R174A
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0.0176
(5R)-5-hydroxylysine
Escherichia coli
pH 8.5, 21°C
0.0016 - 0.12
3-bromo-N-(3-methoxyphenyl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine
0.0025
4,5-trans-dehydrolysine
Escherichia coli
pH 8.5, 21°C
0.0016 - 0.062
4-(2-fluoro-5-methoxyanilino)-5,8-dihydropyrido[2,3-d]pyrimidin-7(6H)-one
0.255
8-azaadenosine-5-triphosphate
Escherichia coli
pH 8.5, 21°C
0.000016
adenosine-5-O-(1-thiotriphosphate)
Escherichia coli
pH 8.5, 21°C
0.000035
alpha,beta-methylene-ATP
Escherichia coli
pH 8.5, 21°C
0.000045
aminoethylcysteine
Escherichia coli
pH 8.5, 21°C
0.0004
aminoethylserine
Escherichia coli
pH 8.5, 21°C
0.105
benzimidazoleriboside-5-triphosphate
Escherichia coli
pH 8.5, 21°C
0.000082
beta,gamma-methyleneadenosine 5'-triphosphate
Escherichia coli
pH 8.5, 21°C
0.91
cadaverine
Escherichia coli
pH 8.5, 21°C
1.77
ethanolamine
Escherichia coli
pH 8.5, 21°C
0.33
histamine
Escherichia coli
pH 8.5, 21°C
0.62
lysinamide
Escherichia coli
pH 8.5, 21°C
0.000085
mutated tRNAIle2
Escherichia coli
pH 8.5, 21°C, C34G-tRNAILe2
-
0.0042 - 0.042
N-(3-methoxyphenyl)-5-methyl-7H-pyrrolo[2,3-d]pyrimidin-4-amine
0.0068
N-acetylethylenediamine
Escherichia coli
pH 8.5, 21°C
1.3
N-alpha-methyl-lysine
Escherichia coli
pH 8.5, 21°C
0.7
ornithine
Escherichia coli
pH 8.5, 21°C
0.0016
3-bromo-N-(3-methoxyphenyl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine
Escherichia coli
-
pH 8.5, temperature not specified in the publication
0.12
3-bromo-N-(3-methoxyphenyl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine
Pseudomonas aeruginosa
-
pH 8.5, temperature not specified in the publication
0.0016
4-(2-fluoro-5-methoxyanilino)-5,8-dihydropyrido[2,3-d]pyrimidin-7(6H)-one
Escherichia coli
-
pH 8.5, temperature not specified in the publication
0.062
4-(2-fluoro-5-methoxyanilino)-5,8-dihydropyrido[2,3-d]pyrimidin-7(6H)-one
Pseudomonas aeruginosa
-
pH 8.5, temperature not specified in the publication
0.0042
N-(3-methoxyphenyl)-5-methyl-7H-pyrrolo[2,3-d]pyrimidin-4-amine
Escherichia coli
-
pH 8.5, temperature not specified in the publication
0.042
N-(3-methoxyphenyl)-5-methyl-7H-pyrrolo[2,3-d]pyrimidin-4-amine
Pseudomonas aeruginosa
-
pH 8.5, temperature not specified in the publication
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malfunction
-
partial inactivation of tilS in vivo results in an AUA codon-dependent translational defect
malfunction
partial inactivation of tilS in vivo results in an AUA codon-dependent translational defect
malfunction
-
the absence of enzyme activity leads to a lack of modification of cytidine34 to lysidine in tRNA2IleLAU, (i.e. synthesis of tRNA2IleCAU), thereby rendering it inactive for translation of AUA codons. Strains of Bacillus subtilis carrying a deletion in the TilS gene can survive only in the presence of a mutant tRNA1Ile, whose anticodon wobble position is changed from G34 to U34 (tRNA1IleUAU)
malfunction
-
the absence of enzyme activity leads to a lack of modification of cytidine34 to lysidine in tRNA2IleLAU, (i.e. synthesis of tRNA2IleCAU), thereby rendering it inactive for translation of AUA codons. Strains of Bacillus subtilis carrying a deletion in the TilS gene can survive only in the presence of a mutant tRNA1Ile, whose anticodon wobble position is changed from G34 to U34 (tRNA1IleUAU)
-
physiological function
-
2-lysyl cytidine is a lysine-containing cytidine derivative commonly found at the wobble position of bacterial AUA codon-specific tRNAIle. This modification determines both codon and amino acid specificities of tRNAIle
physiological function
bacteria decode the isoleucine codon AUA using a tRNA species that is posttranscriptionally modified at the wobble position of the anticodon with a lysine-containing cytidine derivative called lysidine. The lysidine modification of tRNAIle2 is an essential identity determinant for proper aminoacylation by isoleucyl tRNA synthetase and codon recognition on the ribosome. The ATP- and lysine-dependent formation of lysidine is catalyzed by tRNAIle-lysidine synthetase
physiological function
-
enzyme catalyzes the lysylation of C34 in the precursor tRNAIle(CAU), thereby leading to the formation of tRNAIle(lysidineAU). The formation of lysidine by this essential enzyme allows recognition of tRNAIle(lysidineCAU) by Ile-tRNA synthetase and switches the base pairing of the tRNA from AUG (Met) to AUA (Ile). TilS is essential and plays a crucial role in accurate decoding and hence viability of cells
physiological function
-
the enzyme generates lysidine at the wobble position of tRNAIle. The enzyme is essential for the decoding of AUA codons in the cell
physiological function
the enzyme generates lysidine at the wobble position of tRNAIle. The enzyme is essential for the decoding of AUA codons in the cell
physiological function
the single 2-lysylcytidine modification converts the codon-specificity from AUG to AUA, and the amino acid specificity from Met to Ile
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crystal structure of Aquifex aeolicus TilS, complexed with ATP, Mg2+, and L-lysine, at 2.5 A resolution. The presence of the TilS-specific subdomain causes the active site to have two separate gateways, a large hole and a narrow tunnel on the opposite side. ATP is bound inside the hole, and L-lysine is bound at the entrance of the tunnel. The conserved Asp36 in the PP-motif coordinates Mg2+. In these initial binding modes, the ATP, Mg2+, and L-lysine are held far apart from each other, but they seem to be brought together for the reaction upon cytidine binding, with putative structural changes of the complex
crystal structure of TilS at 2.42 A resolution. Structural and functional comparisons with Escherichia coli TilS reveals that the two TilS enzymes discriminate premodified tRNAIle2 from premodified tRNAMet by strategies similar to that used by IleRS, but in distinct manners
structural and functional comparisons of Escherichia coli TilS and Axifex aeolicus TilS reveal that the two TilS enzymes discriminate premodified tRNAIle2 from premodified tRNAMet bystrategies similar to that used by IleRS, but in distinct manners
-
crystal structure of Geobacillus kaustophilus TilS complexed with Bacillus subtilis tRNAIle CAU at 3.65 A resolution, by the multiwavelength anomalous dispersion method. The asymmetric unit contains one TilS homodimer and two tRNAs, each tightly embedded in one monomer of TilS, with an overall interface of 2998 A. Each monomer consists of an amino-terminal catalytic domain, and two carboxy-terminal domains, connected by a long a-helical linker and a loop linker, respectively
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D137A
no activity detectable
D191A
no activity detectable
D36A
no activity detectable
E140A
Km-value for L-lysine is 2.2fold higher than wild-type value, Km-value for ATP is about 7fold higher than wild-type value, Km-value for [tRNAIle2]-cytidine34 is 4.7fold higher than wild-type value
H133A
Km-value for L-lysine is 1.6 fold higher than wild-type value, Km-value for ATP is 2.5fold lower than wild-type value, Km-value for [tRNAIle2]-cytidine34 is similar to wild-type value
N194A
no activity detectable
R113A
no activity detectable
R174A
Km-value for L-lysine is 1.8fold higher than wild-type value, Km-value for ATP is 2.1fold higher than wild-type value, Km-value for [tRNAIle2]-cytidine34 is 6fold higher than wild-type value
R201A
no activity detectable
R205A
Km-value for L-lysine is 1.6fold higher than wild-type value, Km-value for ATP is 14.8fold higher than wild-type value, Km-value for [tRNAIle2]-cytidine34 is 3.6fold higher than wild-type value
S37A
Km-value for ATP is 13fold higher than wild-type value
W188A
Km-value for ATP is 5fold higher than wild-type value
Y114A
Km-value for L-lysine is about 5fold higher than wild-type value, Km-value for ATP is about 8fold higher than wild-type value, Km-value for [tRNAIle2]-cytidine34 is 2.2fold higher than wild-type value
additional information
-
a mutation study reveals that Escherichia coli TilS discriminates tRNAIle from the structurally similar tRNAMet having the same anticodon loop by recognizing the anticodon loop, the anticodon stem, and the acceptor stem
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Suzuki, T.; Miyauchi, K.
Discovery and characterization of tRNAIle lysidine synthetase (TilS)
FEBS Lett.
584
272-277
2010
Escherichia coli (P52097), Escherichia coli
brenda
Salowe, S.P.; Wiltsie, J.; Hawkins, J.C.; Sonatore, L.M.
The catalytic flexibility of tRNAIle-lysidine synthetase can generate alternative tRNA substrates for isoleucyl-tRNA synthetase
J. Biol. Chem.
284
9656-9662
2009
Escherichia coli (P52097), Escherichia coli
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Soma, A.; Ikeuchi, Y.; Kanemasa, S.; Kobayashi, K.; Ogasawara, N.; Ote, T.; Kato, J.; Watanabe, K.; Sekine, Y.; Suzuki, T.
An RNA-modifying enzyme that governs both the codon and amino acid specificities of isoleucine tRNA
Mol. Cell
12
689-698
2003
Escherichia coli, Bacillus subtilis (P37563)
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Ikeuchi, Y.; Soma, A.; Ote, T.; Kato, J.; Sekine, Y.; Suzuki, T.
Molecular mechanism of lysidine synthesis that determines tRNA identity and codon recognition
Mol. Cell
19
235-246
2005
Escherichia coli
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Nakanishi, K.; Bonnefond, L.; Kimura, S.; Suzuki, T.; Ishitani, R.; Nureki, O.
Structural basis for translational fidelity ensured by transfer RNA lysidine synthetase
Nature
461
1144-1148
2009
Geobacillus kaustophilus (Q5L3T3)
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Nakanishi, K.; Fukai, S.; Ikeuchi, Y.; Soma, A.; Sekine, Y.; Suzuki, T.; Nureki, O.
Structural basis for lysidine formation by ATP pyrophosphatase accompanied by a lysine-specific loop and a tRNA-recognition domain.
Proc. Natl. Acad. Sci. USA
102
7487-7492
2005
Escherichia coli, Aquifex aeolicus (O67728), Aquifex aeolicus
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Kuratani, M.; Yoshikawa, Y.; Bessho, Y.; Higashijima, K.; Ishii, T.; Shibata, R.; Takahashi, S.; Yutani, K.; Yokoyama, S.
Structural basis of the initial binding of tRNA(Ile) lysidine synthetase TilS with ATP and L-lysine
Structure
15
1642-1653
2007
Aquifex aeolicus (O67728), Aquifex aeolicus
brenda
Grosjean, H.; Bjrk, G.R.
Enzymatic conversion of cytidine to lysidine in anticodon of bacterial isoleucyl-tRNA - an alternative way of RNA editing
Trends Biochem. Sci.
29
165-168
2004
Escherichia coli
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Taniguchi, T.; Miyauchi, K.; Nakane, D.; Miyata, M.; Muto, A.; Nishimura, S.; Suzuki, T.
Decoding system for the AUA codon by tRNAIle with the UAU anticodon in Mycoplasma mobile
Nucleic Acids Res.
41
2621-2631
2013
no activity in Mycoplasma mobile
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Koehrer, C.; Mandal, D.; Gaston, K.W.; Grosjean, H.; Limbach, P.A.; Rajbhandary, U.L.
Life without tRNAIle-lysidine synthetase: translation of the isoleucine codon AUA in Bacillus subtilis lacking the canonical tRNA2Ile
Nucleic Acids Res.
42
1904-1915
2014
Bacillus subtilis, Bacillus subtilis 168
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Tomikawa, C.; Auxilien, S.; Guerineau, V.; Yoshioka, Y.; Miyoshi, K.; Hori, H.; Fourmy, D.; Takai, K.; Yoshizawa, S.
Characterization of redundant tRNAIles with CAU and UAU anticodons in Lactobacillus plantarum
J. Biochem.
163
233-241
2018
Lactiplantibacillus plantarum (Q88Z33), Lactiplantibacillus plantarum
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Shapiro, A.B.; Plant, H.; Walsh, J.; Sylvester, M.; Hu, J.; Gao, N.; Livchak, S.; Tentarelli, S.; Thresher, J.
Discovery of ATP-competitive inhibitors of tRNAIle lysidine synthetase (TilS) by high-throughput screening
J. Biomol. Screen.
19
1137-1146
2014
Escherichia coli, Pseudomonas aeruginosa
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