Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | the class II enzyme does not show tight product binding and formation of ternary complexes with EF-Tu, it is not activated by EF-Tu | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | thermodynamics, pre-steady-state and single turnover kinetics, steady-state and transient kinetic analyses, recombinant His-tagged enzyme | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Escherichia coli |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP + L-alanine + tRNAAla = AMP + diphosphate + L-alanyl-tRNAAla | kinetic mechanism, AlaRS belongs to the class II of aminoacyl-tRNA ligases due to the position of aminoacylation on the 3'-terminal tRNA ribose, and the topology and tRNAbinding orientation of the active-site protein fold, class II synthetases are rate-limited by a step prior to aminoacyl transfer, the distinct mechanistic signatures of class I versus class II tRNA synthetases ensure rapid turnover of aminoacyl-tRNAs during protein synthesis | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-alanine + tRNAAla | - |
Escherichia coli | AMP + diphosphate + L-alanyl-tRNAAla | - |
? | |
ATP + L-alanine + tRNAAla | a two-step reaction, class II synthetases are rate-limited by a step prior to aminoacyl transfer | Escherichia coli | AMP + diphosphate + L-alanyl-tRNAAla | - |
? |
Synonyms | Comment | Organism |
---|---|---|
alanyl tRNA ligase | - |
Escherichia coli |
More | the enzyme belongs to the MurMN/Fem-ABX family of tRNA-dependent ligases | Escherichia coli |
MurM | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2 | - |
tRNAAla | - |
Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Escherichia coli |