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Literature summary for 6.3.5.6 extracted from
- A single amidotransferase forms asparaginyl-tRNA and glutaminyl-tRNA in Chlamydia trachomatis (2001), J. Biol. Chem., 276, 45862-45867.
Application
| Application | Comment | Organism |
|---|---|---|
| pharmacology | enzyme may have potential as a species-specific therapeutic drug target | Chlamydia trachomatis |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| cloning of the gatC, gatA and gatB genes, situated in an operon-like manner, encoding the GatCAB amidotransferase and overexpression in Escherichia coli BL21-Codon Plus-TM | Chlamydia trachomatis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | not inhibited by N-ethylmaleimide, 5,5Â’-dithiobis(2-nitrobenzoic acid) and p-hydroxymercuribenzoate | Chlamydia trachomatis |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | essential for the reaction catalyzed by AdT | Chlamydia trachomatis |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 53600 | - |
1 * 55000, GatA + 1 * 53600, GatB + 1* 11100, GatC, SDS-PAGE | Chlamydia trachomatis |
| 55000 | - |
1 * 55000, GatA + 1 * 53600, GatB + 1* 11100, GatC, SDS-PAGE | Chlamydia trachomatis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Asp-tRNAAsn + ? | Chlamydia trachomatis | tRNA-dependent transamidation pathway of Asn-tRNA formation, which is required for protein synthesis or under certain metabolic situations for asparagine synthesis | Asn-tRNAAsn + ? | - |
? | |
| Asp-tRNAAsn + ? | Chlamydia trachomatis | it is likely that the dual specificity amidotransferase serves in Asn-tRNA and Gln-tRNA formation in vivo | Asn-tRNAAsn + ? | - |
? | |
| Glu-tRNAGln + ? | Chlamydia trachomatis | it is likely that the dual specificity amidotransferase serves in Asn-tRNA and Gln-tRNA formation in vivo | Gln-tRNAGln + ? | - |
? | |
| Glu-tRNAGln + ? | Chlamydia trachomatis | tRNA-dependent transamidation pathway of Gln-tRNA formation, which is required for protein synthesis or under certain metabolic situations for glutamine synthesis | Gln-tRNAGln + ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Chlamydia trachomatis | - |
human pathogenic parasite | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| 32fold purification of recombinant enzyme, expressed in Escherichia coli | Chlamydia trachomatis |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.000035 | - |
- |
Chlamydia trachomatis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Asp-tRNAAsn + ? | tRNA-dependent transamidation pathway of Asn-tRNA formation, which is required for protein synthesis or under certain metabolic situations for asparagine synthesis | Chlamydia trachomatis | Asn-tRNAAsn + ? | - |
? | |
| Asp-tRNAAsn + ? | it is likely that the dual specificity amidotransferase serves in Asn-tRNA and Gln-tRNA formation in vivo | Chlamydia trachomatis | Asn-tRNAAsn + ? | - |
? | |
| ATP + Asp-tRNAAsn + glutamine | dual-specific Asp/Glu-AdT, rates for conversion of Glu to Gln are about twice as fast as the rate of Asp to Asn conversion, enzyme uses glutamine, asparagine or ammonia as amide donors in the presence of ATP, GTP or CTP | Chlamydia trachomatis | ADP + phosphate + Asn-tRNAAsn + glutamate | - |
? | |
| ATP + Glu-tRNAGln + glutamine | dual-specific Asp/Glu-AdT, rates for conversion of Glu to Gln are about twice as fast as the rate of Asp to Asn conversion, enzyme uses glutamine, asparagine or ammonia as amide donors in the presence of ATP or GTP | Chlamydia trachomatis | ADP + Gln-tRNAGln + glutamate + phosphate | - |
? | |
| Glu-tRNAGln + ? | it is likely that the dual specificity amidotransferase serves in Asn-tRNA and Gln-tRNA formation in vivo | Chlamydia trachomatis | Gln-tRNAGln + ? | - |
? | |
| Glu-tRNAGln + ? | tRNA-dependent transamidation pathway of Gln-tRNA formation, which is required for protein synthesis or under certain metabolic situations for glutamine synthesis | Chlamydia trachomatis | Gln-tRNAGln + ? | - |
? | |
| additional information | GatA is likely to be the catalytic subunit, GatB may be responsible for tRNA binding and GatC may be involved in a channeling mechanism, in which the misacylated tRNA formed by the non-discriminating AA-tRNA synthetase could be handed off to the AdT | Chlamydia trachomatis | ? | - |
? | |
| additional information | no substrates: correctly charged Asp-tRNAAsp and Glu-tRNAGlu | Chlamydia trachomatis | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| heterotrimer | 1 * 55000, GatA + 1 * 53600, GatB + 1* 11100, GatC, SDS-PAGE | Chlamydia trachomatis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Chlamydia trachomatis |
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