Any feedback?
Literature summary for 6.1.1.7 extracted from
- Characterization of zinc-depleted alanyl-tRNA synthetase from Escherichia coli: role of zinc (1999), Arch. Biochem. Biophys., 368, 380-384.
General Stability
| General Stability | Organism |
|---|---|
| Zn2+ stabilizes the enzyme | Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Urea | denaturation at 3.3 M, the Zn2+-depleted enzyme is much more sensitive to denaturation by urea than the native enzyme | Escherichia coli |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | removal of Zn2+ leads to over 50% reduced activity, required for conformational stability and flexibility important for the enzymes activity | Escherichia coli | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 179000 | - |
Zn2+-depleted enzyme, sedimentation coefficient and analytical ultracentrifugation | Escherichia coli |
| 186000 | - |
native enzyme, sedimentation coefficient and analytical ultracentrifugation | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-alanine + tRNAAla | Escherichia coli | - |
AMP + diphosphate + L-alanyl-tRNAAla | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
recombinant wild-type from overexpression in Escherichia coli | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-alanine + tRNAAla | - |
Escherichia coli | AMP + diphosphate + L-alanyl-tRNAAla | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | - |
Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Ala-tRNA synthetase | - |
Escherichia coli |
| Alanine transfer RNA synthetase | - |
Escherichia coli |
| Alanine translase | - |
Escherichia coli |
| Alanine tRNA synthetase | - |
Escherichia coli |
| Alanine-transfer RNA ligase | - |
Escherichia coli |
| alanine-tRNA ligase | - |
Escherichia coli |
| Alanyl-transfer ribonucleate synthetase | - |
Escherichia coli |
| Alanyl-transfer ribonucleic acid synthetase | - |
Escherichia coli |
| Alanyl-transfer RNA synthetase | - |
Escherichia coli |
| Alanyl-tRNA synthetase | - |
Escherichia coli |
| AlaRS | - |
Escherichia coli |
| Synthase, alanyl-transfer ribonucleate | - |
Escherichia coli |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
the Zn2+-depleted enzyme shows reduced viscosity at 10°C compared to 37°C | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Escherichia coli | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
