EC Number | Cloned (Comment) | Organism |
---|---|---|
6.1.1.4 | gene CDC60, expression of wild-type and mutants in an Escherichia coli BL21 strain | Saccharomyces cerevisiae |
6.1.1.4 | gene leuS, expression in a BL21 strain | Escherichia coli |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
6.1.1.4 | crystal growth in presence of mercuric chloride, soaking of the crystals in solution containing 0.6 mM of the non-hydrolyzable substrate analogue norvaline-AMS for 1 month, or cocrystallization of enzyme and norvaline-AMS, X-ray diffraction structure determinationat 2.0-2.2 A resolution and analysis | Thermus thermophilus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
6.1.1.4 | D345A | mutation of the highly conserved Asp residue, located in the CP1 domain, is responsible for editing mechanism, slightly reduced activity with L-leucine, mutant mischarges tRNALeu with isoleucine | Escherichia coli |
6.1.1.4 | D347A | mutation of the highly conserved Asp residue, located in the CP1 domain, is responsible for editing mechanism, slightly reduced activity with L-leucine, mutant mischarges tRNALeu with isoleucine | Thermus thermophilus |
6.1.1.4 | D419A | mutation of the highly conserved Asp residue, located in the CP1 domain, is responsible for editing mechanism, slightly reduced activity with L-leucine, mutant mischarges tRNALeu with isoleucine | Saccharomyces cerevisiae |
6.1.1.4 | T252A | decreased activity with L-leucine, mutant shows altered editing specificity, it edits correctly formed leucyl-tRNALeu | Escherichia coli |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
6.1.1.4 | O-[N-(L-norvalyl)sulfamoyl]adenosine | analogue to the reaction intermediate, non-hydrolyzable | Thermus thermophilus |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
6.1.1.4 | cytoplasm | - |
Saccharomyces cerevisiae | 5737 | - |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.1.1.4 | ATP + L-leucine + tRNALeu | Escherichia coli | - |
AMP + diphosphate + L-leucyl-tRNALeu | - |
r | |
6.1.1.4 | ATP + L-leucine + tRNALeu | Saccharomyces cerevisiae | - |
AMP + diphosphate + L-leucyl-tRNALeu | - |
r | |
6.1.1.4 | ATP + L-leucine + tRNALeu | Thermus thermophilus | - |
AMP + diphosphate + L-leucyl-tRNALeu | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
6.1.1.4 | Escherichia coli | - |
- |
- |
6.1.1.4 | Saccharomyces cerevisiae | - |
- |
- |
6.1.1.4 | Thermus thermophilus | Q72GM3 | purified recombinant enzyme | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
6.1.1.4 | recombinant enzyme | Escherichia coli |
6.1.1.4 | recombinant from Escherichia coli | Saccharomyces cerevisiae |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
6.1.1.4 | ATP + L-leucine + tRNALeu = AMP + diphosphate + L-leucyl-tRNALeu | active site structure and mechanism, the editing active site binds the two different substrates using a single amino acid discriminatory pocket while preserving he same mode of adenine recognition, Asp347 is involved in the editing process, mechanism of hydrolysis | Thermus thermophilus | |
6.1.1.4 | ATP + L-leucine + tRNALeu = AMP + diphosphate + L-leucyl-tRNALeu | Asp345 is involved in the editing process, mechanism of hydrolysis | Escherichia coli | |
6.1.1.4 | ATP + L-leucine + tRNALeu = AMP + diphosphate + L-leucyl-tRNALeu | Asp419 is involved in the editing process, mechanism of hydrolysis | Saccharomyces cerevisiae |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.1.1.4 | ATP + L-isoleucine + tRNALeu | mutant D345A, not the wild-type which performs only the misacetylation with isoleucine, but eliminates the incorrect isoleucyl-AMP | Escherichia coli | AMP + diphosphate + L-isoleucyl-tRNALeu | - |
r | |
6.1.1.4 | ATP + L-isoleucine + tRNALeu | mutant D345A, not the wild-type which performs only the misacetylation with isoleucine, but eliminates the incorrect isoleucyl-AMP | Thermus thermophilus | AMP + diphosphate + L-isoleucyl-tRNALeu | - |
r | |
6.1.1.4 | ATP + L-isoleucine + tRNALeu | mutant D419A, not the wild-type, which performs only the misacetylation with isoleucine, but eliminates the incorrect isoleucyl-AMP | Saccharomyces cerevisiae | AMP + diphosphate + L-isoleucyl-tRNALeu | - |
r | |
6.1.1.4 | ATP + L-leucine + tRNALeu | - |
Escherichia coli | AMP + diphosphate + L-leucyl-tRNALeu | - |
r | |
6.1.1.4 | ATP + L-leucine + tRNALeu | - |
Saccharomyces cerevisiae | AMP + diphosphate + L-leucyl-tRNALeu | - |
r | |
6.1.1.4 | ATP + L-leucine + tRNALeu | - |
Thermus thermophilus | AMP + diphosphate + L-leucyl-tRNALeu | - |
r | |
6.1.1.4 | ATP + L-leucine + tRNALeu | mutant T252A edits correctly charged Leu-tRNALeu | Escherichia coli | AMP + diphosphate + L-leucyl-tRNALeu | - |
r | |
6.1.1.4 | ATP + L-leucine + tRNALeu | the editing active site hydrolytically cleaves the misactivated aminoacyl-adenylate, called pre-transfer editing, or the mischarged tRNA, called post-transfer editing | Thermus thermophilus | AMP + diphosphate + L-leucyl-tRNALeu | - |
r | |
6.1.1.4 | ATP + L-methionine + tRNALeu | mutant D345A, not the wild-type enzyme | Escherichia coli | AMP + diphosphate + L-methionyl-tRNALeu | - |
r | |
6.1.1.4 | ATP + L-methionine + tRNALeu | mutant D419A, not the wild-type enzyme | Saccharomyces cerevisiae | AMP + diphosphate + L-methionyl-tRNALeu | - |
r |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
6.1.1.4 | Leucine translase | - |
Escherichia coli |
6.1.1.4 | Leucine translase | - |
Saccharomyces cerevisiae |
6.1.1.4 | Leucine translase | - |
Thermus thermophilus |
6.1.1.4 | Leucine--tRNA ligase | - |
Escherichia coli |
6.1.1.4 | Leucine--tRNA ligase | - |
Saccharomyces cerevisiae |
6.1.1.4 | Leucine--tRNA ligase | - |
Thermus thermophilus |
6.1.1.4 | Leucyl-transfer ribonucleate synthetase | - |
Escherichia coli |
6.1.1.4 | Leucyl-transfer ribonucleate synthetase | - |
Saccharomyces cerevisiae |
6.1.1.4 | Leucyl-transfer ribonucleate synthetase | - |
Thermus thermophilus |
6.1.1.4 | Leucyl-transfer ribonucleic acid synthetase | - |
Escherichia coli |
6.1.1.4 | Leucyl-transfer ribonucleic acid synthetase | - |
Saccharomyces cerevisiae |
6.1.1.4 | Leucyl-transfer ribonucleic acid synthetase | - |
Thermus thermophilus |
6.1.1.4 | Leucyl-transfer RNA synthetase | - |
Escherichia coli |
6.1.1.4 | Leucyl-transfer RNA synthetase | - |
Saccharomyces cerevisiae |
6.1.1.4 | Leucyl-transfer RNA synthetase | - |
Thermus thermophilus |
6.1.1.4 | Leucyl-tRNA synthetase | - |
Escherichia coli |
6.1.1.4 | Leucyl-tRNA synthetase | - |
Saccharomyces cerevisiae |
6.1.1.4 | Leucyl-tRNA synthetase | - |
Thermus thermophilus |
6.1.1.4 | LeuRS | - |
Escherichia coli |
6.1.1.4 | LeuRS | - |
Saccharomyces cerevisiae |
6.1.1.4 | LeuRS | - |
Thermus thermophilus |
6.1.1.4 | LeuRSTT | - |
Thermus thermophilus |
6.1.1.4 | Synthetase, leucyl-transfer ribonucleate | - |
Escherichia coli |
6.1.1.4 | Synthetase, leucyl-transfer ribonucleate | - |
Saccharomyces cerevisiae |
6.1.1.4 | Synthetase, leucyl-transfer ribonucleate | - |
Thermus thermophilus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
6.1.1.4 | 7.5 | - |
assay at | Escherichia coli |
6.1.1.4 | 7.5 | - |
assay at | Saccharomyces cerevisiae |
6.1.1.4 | 7.5 | - |
assay at | Thermus thermophilus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
6.1.1.4 | ATP | - |
Escherichia coli | |
6.1.1.4 | ATP | - |
Saccharomyces cerevisiae | |
6.1.1.4 | ATP | - |
Thermus thermophilus |