EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
    6.1.1.9 | 2-chloroadenosine 5'-triphosphate + L-valine + tRNAVal |
- |
Saccharomyces cerevisiae |
2-chloroadenosine 5'-monophosphate + diphosphate + L-valyl-tRNAVal |
- |
? |
| 6.1.1.9 | ATP + DL-2-amino-3-chlorobutyrate + tRNAVal |
as effective as valine |
Escherichia coli |
AMP + diphosphate + DL-2-amino-3-chlorobutyryl-tRNAVal |
- |
? |
| 6.1.1.9 | ATP + DL-2-aminobutyrate + tRNAVal |
30% of the activity with valine |
Escherichia coli |
AMP + diphosphate + DL-2-aminobutyryl-tRNAVal |
- |
? |
| 6.1.1.9 | ATP + DL-allo-2-amino-3-chlorobutyrate + tRNAVal |
15% of the activity with valine |
Escherichia coli |
AMP + diphosphate + DL-allo-2-amino-3-chlorobutyryl-tRNAVal |
- |
? |
| 6.1.1.9 | ATP + DL-threonine + tRNAVal |
- |
Escherichia coli |
AMP + diphosphate + DL-threonyl-tRNAVal |
- |
? |
| 6.1.1.9 | ATP + L-isoleucine + tRNAVal |
very low activity |
Escherichia coli |
AMP + diphosphate + L-isoleucyl-tRNAVal |
- |
? |
| 6.1.1.9 | ATP + L-threonine + tRNAVal |
28% of the activity with valine |
Escherichia coli |
AMP + diphosphate + L-threonyl-tRNAVal |
- |
? |
| 6.1.1.9 | ATP + L-threonine + tRNAVal |
noncognate isosteric substrate, low activity, posttransfer editing occurs |
Escherichia coli |
AMP + diphosphate + L-threonyl-tRNAVal |
- |
ir |
| 6.1.1.9 | ATP + L-threonine + tRNAVal |
1 step performance of an originally two-step reaction, the enzyme can hardly differentiate between the cognate amino acid valine and others, especially threonine, to minimize misaminoacetylation the enzyme performs a proofreading, socalled editing reaction at a second active site, which is dependent on the presence of cognate tRNAVal whose 3'-end is involved in the editing reaction, a majority of editing by the enzyme entails prior charging of the tRNA, misacylated tRNA is a transient intermediate in the editing reaction |
Escherichia coli |
? |
- |
? |
| 6.1.1.9 | ATP + L-valine + tRNAiMet,GAC mutant |
anticodon CAU to GAC initiator tRNA mutant, i.e. G34C36 mutant, is aminoacylated in vitro and in vivo, its anticodon sequence corresponds to the one of tRNAVal |
Haloferax volcanii |
AMP + diphosphate + L-valyl-tRNAiMet,GAC mutant |
- |
? |
