6.1.1.5: isoleucine-tRNA ligase
This is an abbreviated version!
For detailed information about isoleucine-tRNA ligase, go to the full flat file.
Word Map on EC 6.1.1.5
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6.1.1.5
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synthetases
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aminoacyl-trna
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aminoacylation
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isoleucylation
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valyl-trna
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misactivated
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methionyl-trna
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leurs
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mischarged
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pseudomonic
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post-transfer
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noncognate
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valrs
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mupirocin-resistant
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misacylated
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anticodons
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aarss
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kmsks
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glnrs
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trna-dependent
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pretransfer
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lysyl-trna
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molecular biology
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medicine
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drug development
- 6.1.1.5
- synthetases
- aminoacyl-trna
- aminoacylation
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isoleucylation
- valyl-trna
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misactivated
- methionyl-trna
- leurs
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mischarged
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pseudomonic
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post-transfer
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noncognate
- valrs
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mupirocin-resistant
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misacylated
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anticodons
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aarss
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kmsks
- glnrs
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trna-dependent
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pretransfer
- lysyl-trna
- molecular biology
- medicine
- drug development
Reaction
Synonyms
EcIleRS, IARS2, Ile-tRNA synthetase, IleRS, ileS, ileS1, ileS2, IRS, Isoleucine translase, Isoleucine--tRNA ligase, Isoleucine-transfer RNA ligase, Isoleucine-tRNA synthetase, isoleucyl tRNA synthetase, Isoleucyl-transfer ribonucleate synthetase, Isoleucyl-transfer RNA synthetase, Isoleucyl-tRNA synthetase, mitochondrial isoleucyl-tRNA synthetase, More, mt isoleucyl-tRNA synthetase, mt-IleRS, Mupirocin resistance protein, ScIleRS, SgIleRS, Synthetase, isoleucyl-transfer ribonucleate
ECTree
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Substrates Products
Substrates Products on EC 6.1.1.5 - isoleucine-tRNA ligase
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REACTION DIAGRAM
ATP + L-valine + tRNAIle
AMP + diphosphate + L-valyl-tRNAIle
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CP1 domain of the enzyme deacylates or edits the mischarged Val-tRNAIle
r
Ile-tRNAIle + 3-mercaptopropionate
S-Isoleucyl-3-mercaptopropionate + tRNAIle
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-
-
?
Ile-tRNAIle + cysteine
tRNAIle + isoleucylcysteine
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D- and L-isomer of Lys
D-isoleucylcysteine and L-isoleucylcysteine
?
Ile-tRNAIle + L-cysteine methyl ester
tRNAIle + isoleucyl-L-cysteine methyl ester
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-
-
?
Ile-tRNAIle + N-acetylcysteine
S-isoleucyl-N-acetylcysteine + tRNAIle
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-
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?
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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 IleRS
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-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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 IleRS
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-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
Bacillus subtilis BAL4574
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-
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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the reaction plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
-
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
-
r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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the anticodon for methionine and isoleucine tRNAs differ by a single nucleotide, changing this nucleotide in an isoleucine tRNA is sufficient to change aminoacylation specificity to methionine
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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formation of an aminoacyl adenylate reaction intermediate
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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the binding region of the adenine moiety contains a wide hydrophobic pocket large enough to afford three linear aromatic rings
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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physiological function is Thr formation of Ile-tRNA and editing of inadvertently misactivated homocysteine
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-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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a two-step reaction, the first of which, the amino acid activation step, is reversible, while the second aminoacylation step is not, the amino acid editing site for LeuRS resides within the homologous CP1 domain containing a conserved threonine conferring amino acid substrate recognition, editing mechanism, some positions of the site are idiosyncratic to IleRS, residues Arg249, Asp251, Thr252, Met336, and Val338 are involved,overview
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-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
usage of purified recombinant tRNAGAU Ile (with G1-C72 instead of the wild-type A1-U72 sequence) overexpressed in Escherichia coli strain BL21(DE3)
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
Escherichia coli B / ATCC 11303
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-
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
Escherichia coli B / ATCC 11303
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-
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
Escherichia coli B / ATCC 11303
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-
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
Escherichia coli B / ATCC 11303
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-
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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0.3% or less of the activity with isoleucine is measured with other amino acids
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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the reaction catalyzed by the enzyme plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
tRNAIle from Pseudomonas fluorescens and Escherichia coli
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
tRNAIle from Pseudomonas fluorescens and Escherichia coli
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
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r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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enzyme has specificity for E. coli tRNAIle
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
Saccharomyces cerevisiae ATCC 204508 / S288c
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-
-
r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
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r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
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r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
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r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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-
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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formation of a enzyme-bound aminoacyl adenylate intermediate
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r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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reaction intermediate is the Ile-AMP-enzyme complex
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r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
Streptococcus pneumoniae D39 / NCTC 7466
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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enzyme shows a common recognition mode of aminoacyl-adenylate for a class I aminoacyl-tRNA synthetase, formation of high-energy reaction intermediate Ile-AMP
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
substrate recognition mechanisms of IleRS are characterized by the active-site rearrangement between the two editing modes, overview, the editing domain contributes to accurate aminoacylation by hydrolyzing the mis-synthesized intermediate, valyl-adenylate, in the pre-transfer editing mode and the incorrect final product, valyl-tRNAIle, in the post-transfer editing mode, Trp227 with its aromatic ring is important
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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enzyme shows a common recognition mode of aminoacyl-adenylate for a class I aminoacyl-tRNA synthetase, formation of high-energy reaction intermediate Ile-AMP
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
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?
?
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aminoacyl-tRNA is channeled in vivo by probably direct transfer to elongation factor I
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?
additional information
?
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discrimination of 20 amino acids in aminoacylation of modified tRNAIle-C-C-A(3'NH2)
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?
additional information
?
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Ile + ATP + enzyme/Ile-AMP-enzyme + diphosphate, isoleucine-dependent ATP-diphosphate exchange
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?
additional information
?
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Ile + ATP + enzyme/Ile-AMP-enzyme + diphosphate, isoleucine-dependent ATP-diphosphate exchange
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?
additional information
?
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Ile + ATP + enzyme/Ile-AMP-enzyme + diphosphate, isoleucine-dependent ATP-diphosphate exchange
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?
additional information
?
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Ile + ATP + enzyme/Ile-AMP-enzyme + diphosphate, isoleucine-dependent ATP-diphosphate exchange
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?
additional information
?
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enzymatic reactions catalyzed by IleRS include amino acid activation, tRNA binding, aminoacyl transfer, and dissociation of aminoacylated tRNA from the enzyme, in the synthetic pathway. Pretransfer editing may proceed through enhanced dissociation of noncognate aminoacyl-AMP (1) or through its enzymatic hydrolysis, which may be tRNA-independent (2) ortRNA-dependent (3). Misacylated tRNA is deacylated through posttransferediting, overview
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?
additional information
?
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enzymatic reactions catalyzed by IleRS include amino acid activation, tRNA binding, aminoacyl transfer, and dissociation of aminoacylated tRNA from the enzyme, in the synthetic pathway. Pretransfer editing may proceed through enhanced dissociation of noncognate aminoacyl-AMP (1) or through its enzymatic hydrolysis, which may be tRNA-independent (2) ortRNA-dependent (3). Misacylated tRNA is deacylated through posttransferediting, overview
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?
additional information
?
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wild-type an dmutant enzymes IleRS are tested in reactions with both L-valine and L-isoleucine, neither wild-type nor D342A IleRS significantly deacylates Ile-tRNAIle under steady-state conditions
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?
additional information
?
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wild-type an dmutant enzymes IleRS are tested in reactions with both L-valine and L-isoleucine, neither wild-type nor D342A IleRS significantly deacylates Ile-tRNAIle under steady-state conditions
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?
additional information
?
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Escherichia coli B / ATCC 11303
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Ile + ATP + enzyme/Ile-AMP-enzyme + diphosphate, isoleucine-dependent ATP-diphosphate exchange
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?
additional information
?
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discrimination of 20 amino acids in aminoacylation of modified tRNAIle-C-C-A(3'NH2)
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?
additional information
?
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Ile + ATP + enzyme/Ile-AMP-enzyme + diphosphate, isoleucine-dependent ATP-diphosphate exchange
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?
additional information
?
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aminoacyl-tRNA is channeled in vivo by probably direct transfer to elongation factor I
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?
additional information
?
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position 2,6,7,8,9,2' and 3' of ATP are important for catalytic action of isleucyl-tRNA synthetase
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?
additional information
?
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discrimination of 20 amino acids in aminoacylation of modified tRNAIle-C-C-A(3'NH2)
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?
additional information
?
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Ile + ATP + enzyme/Ile-AMP-enzyme + diphosphate, isoleucine-dependent ATP-diphosphate exchange
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?
additional information
?
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the enzyme is also active with L-valine instead of L-isoleucine
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?
additional information
?
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the enzyme is also active with L-valine instead of L-isoleucine
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?
additional information
?
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analysed are ATP-PPi exchange assay, aminoacylation, and editing in the presence of tRNA of the recombinant wild-type and mutant enzymes. The enzyme is also active with L-valine instead of L-isoleucine, kinetics
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?
additional information
?
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analysed are ATP-PPi exchange assay, aminoacylation, and editing in the presence of tRNA of the recombinant wild-type and mutant enzymes. The enzyme is also active with L-valine instead of L-isoleucine, kinetics
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additional information
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Saccharomyces cerevisiae ATCC 204508 / S288c
the enzyme is also active with L-valine instead of L-isoleucine
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?
additional information
?
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Saccharomyces cerevisiae ATCC 204508 / S288c
analysed are ATP-PPi exchange assay, aminoacylation, and editing in the presence of tRNA of the recombinant wild-type and mutant enzymes. The enzyme is also active with L-valine instead of L-isoleucine, kinetics
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?
additional information
?
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enzyme also performs the reversible ATP-diphosphate exchange reaction
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?
additional information
?
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enzyme also performs the reversible ATP-diphosphate exchange reaction
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additional information
?
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enzyme also performs the reversible ATP-diphosphate exchange reaction
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?
additional information
?
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pneumococcal enzyme IleRS robustly mischarges its cognate tRNA with Leu and Val, comparative Streptomyces pneumoniae IleRS-catalyzed (mis)charging of wild-type and G16C tRNAIle with isoleucine, leucine, or valine, overview. IleRS has a weak posttransfer editing activity against LeutRNAIle. The G16C mutation in pneumococcal tRNAIle, is implicated in the editing of Val-tRNAIle by IleRS
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?
additional information
?
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pneumococcal enzyme IleRS robustly mischarges its cognate tRNA with Leu and Val, comparative Streptomyces pneumoniae IleRS-catalyzed (mis)charging of wild-type and G16C tRNAIle with isoleucine, leucine, or valine, overview. IleRS has a weak posttransfer editing activity against LeutRNAIle. The G16C mutation in pneumococcal tRNAIle, is implicated in the editing of Val-tRNAIle by IleRS
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additional information
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analysis of the aminoacylation profiles of class I isoleucyl-tRNA synthetase (IleRS)
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?
additional information
?
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analysis of the aminoacylation profiles of class I isoleucyl-tRNA synthetase (IleRS)
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?
additional information
?
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Streptococcus pneumoniae D39 / NCTC 7466
pneumococcal enzyme IleRS robustly mischarges its cognate tRNA with Leu and Val, comparative Streptomyces pneumoniae IleRS-catalyzed (mis)charging of wild-type and G16C tRNAIle with isoleucine, leucine, or valine, overview. IleRS has a weak posttransfer editing activity against LeutRNAIle. The G16C mutation in pneumococcal tRNAIle, is implicated in the editing of Val-tRNAIle by IleRS
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additional information
?
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Streptococcus pneumoniae D39 / NCTC 7466
analysis of the aminoacylation profiles of class I isoleucyl-tRNA synthetase (IleRS)
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?
additional information
?
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the enzyme is also active with L-valine instead of L-isoleucine
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?
additional information
?
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the enzyme is also active with L-valine instead of L-isoleucine, kinetics
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?
additional information
?
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Ile + ATP + enzyme/Ile-AMP-enzyme + diphosphate, isoleucine-dependent ATP-diphosphate exchange
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?
additional information
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Thr233 and His319 recognize the substrate valine side-chain, regardless of the valine side-chain rotation, and reject the isoleucine side-chain
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additional information
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Thr233 and His319 recognize the substrate valine side-chain, regardless of the valine side-chain rotation, and reject the isoleucine side-chain
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?
additional information
?
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Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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Ile + ATP + enzyme/Ile-AMP-enzyme + diphosphate, isoleucine-dependent ATP-diphosphate exchange
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-
?