6.3.4.19: tRNAIle-lysidine synthase
This is an abbreviated version!
For detailed information about tRNAIle-lysidine synthase, go to the full flat file.
Word Map on EC 6.3.4.19
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6.3.4.19
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isoleucine
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anticodons
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wobble
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decode
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aminoacylation
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aquifex
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ilers
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analysis
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aeolicus
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hole
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pyrophosphatase
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trnamet
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isoleucyl-trna
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methionyl-trna
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medicine
- 6.3.4.19
- isoleucine
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anticodons
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wobble
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decode
- aminoacylation
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aquifex
- ilers
- analysis
- aeolicus
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hole
- pyrophosphatase
- trnamet
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isoleucyl-trna
- methionyl-trna
- medicine
Reaction
Synonyms
lysidine synthetase, mesJ, MesJ protein, TilS, TilS protein, tRNAIle lysidine synthetase, tRNAIle-lysidine synthetase, yacA
ECTree
6.3.4.19 tRNAIle-lysidine synthaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 6.3.4.19 - tRNAIle-lysidine synthase
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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
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
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-
?
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
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-
?
[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
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-
?
[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
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-
?
[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
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-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
[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
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-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
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-
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?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
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-
-
-
?
[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
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-
?
[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
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-
?
[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
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-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
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-
-
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
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-
-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
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-
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?
[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
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?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
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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)
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-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
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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
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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
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-
?
[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
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-
?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
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-
-
?
[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
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-
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?
[tRNAIle2]-cytidine34 + L-lysine + ATP
[tRNAIle2]-lysidine34 + AMP + diphosphate + H2O
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?
additional information
?
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no substrate: N1-methyladenosine-5'-triphosphate, 2-aminoadenosine-5'-triphosphate, 2-amino-6-chloropurineriboside-5'-triphosphate, and 6-chloropurineriboside-5'-triphosphate
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-
?
additional information
?
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no substrate: N1-methyladenosine-5'-triphosphate, 2-aminoadenosine-5'-triphosphate, 2-amino-6-chloropurineriboside-5'-triphosphate, and 6-chloropurineriboside-5'-triphosphate
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-
?
