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Literature summary for 2.7.7.87 extracted from
- Mechanism of N6-threonylcarbamoyladenonsine (t6A) biosynthesis: isolation and characterization of the intermediate threonylcarbamoyl-AMP (2012), Biochemistry, 51, 8950-8963.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| SDS-PAGE, cloning of ywlC and ydiB as His6 N-fusion proteins and highly expression in Escherichia coli BL21(DE3), because of inclusion bodies construction of N-terminal thioredoxin (trxA) fusion proteins of ydiC and ydiE, which allow good expression and sufficient solubility for in vitro studies | Bacillus subtilis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-threonine + ATP + CO2 | Bacillus subtilis | catalyzed by YwlC(TsaC) | L-threonylcarbamoyl-AMP + diphosphate | L-threonylcarbamoyl-AMP i.e. TC-AMP, isolated by HPLC and characterized by mass spectrometry and 1H-NMR | ? |  |
| L-threonine + ATP + CO2 | Bacillus subtilis 168 | catalyzed by YwlC(TsaC) | L-threonylcarbamoyl-AMP + diphosphate | L-threonylcarbamoyl-AMP i.e. TC-AMP, isolated by HPLC and characterized by mass spectrometry and 1H-NMR | ? | |
| L-threonylcarbamoyl-AMP + tRNA | Bacillus subtilis | catalyzed by YdiBCE(TsaEBD), a study of RNA substrate specificity shows that tRNA(Thr) and tRNA(Lys) are modified, whereas tRNA(Phe) is not modified | t6A37-tRNA | - |
? | |
| L-threonylcarbamoyl-AMP + tRNA | Bacillus subtilis 168 | catalyzed by YdiBCE(TsaEBD), a study of RNA substrate specificity shows that tRNA(Thr) and tRNA(Lys) are modified, whereas tRNA(Phe) is not modified | t6A37-tRNA | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | P39153 | - |
- |
| Bacillus subtilis 168 | P39153 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| attempts to purify the native forms of YdiC and YdiE by specific cleavage of the fusion proteins with thrombin or Factor Xa protease lead to multiple products, perhaps because the proteins are not completely stable in the cleavage reaction conditions | Bacillus subtilis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-threonine + ATP + CO2 | catalyzed by YwlC(TsaC) | Bacillus subtilis | L-threonylcarbamoyl-AMP + diphosphate | L-threonylcarbamoyl-AMP i.e. TC-AMP, isolated by HPLC and characterized by mass spectrometry and 1H-NMR | ? | |
| L-threonine + ATP + CO2 | catalyzed by YwlC(TsaC) | Bacillus subtilis 168 | L-threonylcarbamoyl-AMP + diphosphate | L-threonylcarbamoyl-AMP i.e. TC-AMP, isolated by HPLC and characterized by mass spectrometry and 1H-NMR | ? | |
| L-threonylcarbamoyl-AMP + tRNA | catalyzed by YdiBCE(TsaEBD), a study of RNA substrate specificity shows that tRNA(Thr) and tRNA(Lys) are modified, whereas tRNA(Phe) is not modified | Bacillus subtilis | t6A37-tRNA | - |
? | |
| L-threonylcarbamoyl-AMP + tRNA | catalyzed by YdiBCE(TsaEBD), a study of RNA substrate specificity shows that tRNA(Thr) and tRNA(Lys) are modified, whereas tRNA(Phe) is not modified | Bacillus subtilis 168 | t6A37-tRNA | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| YwlC | - |
Bacillus subtilis |
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